All structure family : SET domain
 
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Entries released this week  (1)
revised
(2)
 
Entry Information
Entry status  (1)
REL
(187)
 
Experimental methods  (2)
X-ray diffraction
(184)
Solution NMR
(3)
 
Authors  (722)
Arrowsmith CH
(50)
Edwards AM
(39)
Structural Genomics Consortium (SGC)
(39)
Vedadi M
(37)
Brown PJ
(35)
Wu H
(35)
Bountra C
(32)
Zeng H
(30)
Dong A
(28)
Trievel RC
(26)
Couture JF
(23)
Min J
(23)
Li F
(21)
Houtz RL
(20)
Weigelt J
(19)
Brunzelle JS
(18)
Couture J-F
(17)
Cheng X
(16)
Dirk LM
(16)
Jin J
(16)
Loppnau P
(15)
Wu J
(15)
Babault N
(14)
Liu J
(14)
Tempel W
(14)
Allali-Hassani A
(12)
Bochkarev A
(12)
Li Y
(12)
Schapira M
(12)
Dombrovski L
(11)
Horton JR
(11)
Plotnikov AN
(11)
Zhang X
(11)
Chen H
(10)
Chen X
(10)
Li S
(10)
Xiong Y
(10)
Yu W
(10)
Del Rizzo PA
(9)
Wilson JR
(9)
Cheung T
(8)
Ferguson AD
(8)
Garcia-Arenas R
(8)
Godin R
(8)
Howard T
(8)
Keen N
(8)
Larsen NA
(8)
Luo M
(8)
Roiko MS
(8)
Strunk BS
(8)
Antoshenko T
(7)
Chang Y
(7)
Du J
(7)
Jacobsen SE
(7)
Lunin VV
(7)
Amaya MF
(6)
Barsyte-Lovejoy D
(6)
Bedford MT
(6)
Blackburn GM
(6)
Campagna-Slater V
(6)
Dirk LMA
(6)
Siarheyeva A
(6)
Sundstrom M
(6)
Wang J
(6)
Yang Z
(6)
Barsyte D
(5)
Bergamin E
(5)
Blum G
(5)
Brunzelle J
(5)
Chen Y
(5)
Cho HJ
(5)
Cierpicki T
(5)
Eram MS
(5)
Gamblin SJ
(5)
Grembecka J
(5)
Hauk G
(5)
Horowitz S
(5)
Maillard I
(5)
Michaels SD
(5)
Mongeon V
(5)
Ndoj J
(5)
Pittella-Silva F
(5)
Rogawski DS
(5)
Shinkai Y
(5)
Sirinupong N
(5)
Walker JR
(5)
Xu RM
(5)
Zhang Y
(5)
Zhou MM
(5)
Al-Hashimi HM
(4)
Allis CD
(4)
Baburajendran N
(4)
Bellon S
(4)
Bellon SF
(4)
Blais A
(4)
Bunnage M
(4)
Cantone N
(4)
Cao F
(4)
Cao L
(4)
Chen J
(4)
 
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Homo / hetero assembly  (2)
homo
(124)
hetero
(63)
 
Assembly composition  (3)
protein structure
(124)
protein/protein complex
(59)
DNA/protein complex
(4)
 
Assembly polymer count  (7)
monomer
(99)
dimer
(74)
tetramer
(7)
trimer
(4)
heptamer
(1)
octamer
(1)
pentamer
(1)
 
Resolution distribution
1.0 - 1.5
(13)
1.5 - 2
(79)
2.0 - 2.5
(62)
2.5 - 3
(25)
3.0 - 3.5
(4)
3.5 - 4
(1)
 
Release year distribution
2000 - 2005
(17)
2005 - 2010
(50)
2010 - 2015
(78)
2015 - 2020
(74)
 
Journal  (30)
To be published
(24)
J Biol Chem
(20)
J Med Chem
(16)
Proc Natl Acad Sci U S A
(16)
PLoS One
(12)
Mol Cell
(9)
Nature
(9)
Nucleic Acids Res
(9)
Nat Struct Biol
(7)
Structure
(7)
ACS Med Chem Lett
(6)
J Mol Biol
(6)
Biochemistry
(5)
J Am Chem Soc
(5)
ACS Chem Biol
(4)
Bioorg Med Chem
(4)
Cell
(4)
Elife
(4)
Nat Struct Mol Biol
(3)
Acta Crystallogr D Biol Crystallogr
(2)
EMBO J
(2)
FEBS Lett
(2)
Genes Dev
(2)
Nat Chem Biol
(2)
Nat Commun
(2)
Biochem Biophys Res Commun
(1)
Cell Rep
(1)
ChemMedChem
(1)
J Mol Cell Biol
(1)
Science
(1)
 
Macromolecules
Organism superkingdom  (2)
Eukaryota
(182)
Viruses
(5)
 
Organism name  (12)
Homo sapiens
(148)
Arabidopsis thaliana
(7)
Pisum sativum
(7)
Mus musculus
(6)
Paramecium bursaria Chlorella virus 1
(5)
Ricinus communis
(5)
Neurospora crassa
(2)
Schizosaccharomyces pombe
(2)
Schizosaccharomyces pombe 972h-
(2)
Cryptosporidium parvum Iowa II
(1)
Kluyveromyces lactis NRRL Y-1140
(1)
Plasmodium (Laverania)
(1)
 
Molecule name  (204)
H3-K4-HMTase SETD7
(32)
Histone H3-K4 methyltransferase SETD7
(32)
Histone-lysine N-methyltransferase SETD7
(32)
Lysine N-methyltransferase 7
(32)
SET domain-containing protein 7
(32)
SET7/9
(32)
Histone methyltransferase SMYD2
(19)
N-lysine methyltransferase SMYD2
(19)
SET and MYND domain-containing protein 2
(19)
Histone-lysine N-methyltransferase SMYD3
(18)
SET and MYND domain-containing protein 3
(18)
Zinc finger MYND domain-containing protein 1
(18)
Eu-HMTase1
(17)
Euchromatic histone-lysine N-methyltransferase 1
(17)
G9a-like protein 1
(17)
GLP
(17)
GLP1
(17)
H3-K9-HMTase 5
(17)
HSKM-B
(17)
Histone H3-K9 methyltransferase 5
(17)
Histone-lysine N-methyltransferase EHMT1
(17)
Lysine N-methyltransferase 1D
(17)
Lysine N-methyltransferase 3C
(17)
Euchromatic histone-lysine N-methyltransferase 2
(15)
H3-K9-HMTase 3
(15)
HLA-B-associated transcript 8
(15)
Histone H3-K9 methyltransferase 3
(15)
Histone-lysine N-methyltransferase EHMT2
(15)
Lysine N-methyltransferase 1C
(15)
Protein G9a
(15)
H4-K20-HMTase KMT5A
(13)
Histone-lysine N-methyltransferase KMT5A
(13)
Lysine N-methyltransferase 5A
(13)
Lysine-specific methylase 5A
(13)
N-lysine methyltransferase KMT5A
(13)
PR-Set7
(13)
PR/SET domain-containing protein 07
(13)
PR/SET07
(13)
SET domain-containing protein 8
(13)
PsLSMT
(7)
Ribulose-1,5 bisphosphate carboxylase/oxygenase large subunit N-methyltransferase, chloroplastic
(7)
RuBisCO LSMT
(7)
RuBisCO methyltransferase
(7)
SET domain-containing protein
(7)
[Fructose-bisphosphate aldolase]-lysine N-methyltransferase
(7)
[Ribulose-bisphosphate carboxylase]-lysine N-methyltransferase
(7)
rbcMT
(7)
ASH1-like protein
(6)
Absent small and homeotic disks protein 1 homolog
(6)
HKMT
(6)
Histone-lysine N-methyltransferase ASH1L
(6)
Lysine N-methyltransferase 2H
(6)
[histone H4]-N-methyl-L-lysine20 N-methyltransferase KMT5B
(6)
[histone H4]-lysine20 N-methyltransferase KMT5B
(6)
huASH1
(6)
Histone H3K27 methylase
(5)
Probable Histone-lysine N-methyltransferase ATXR5
(5)
ALL-1
(4)
C-terminal cleavage product of 180 kDa
(4)
CXXC-type zinc finger protein 7
(4)
Cryptic loci regulator 4
(4)
Cysteine methyltransferase KMT2A
(4)
H3-K9-HMTase
(4)
HIF-1
(4)
HIP-1
(4)
Histone H3-K9 methyltransferase
(4)
Histone-lysine N-methyltransferase 2A
(4)
Histone-lysine N-methyltransferase KMT5B
(4)
Histone-lysine N-methyltransferase SETD2
(4)
Histone-lysine N-methyltransferase, H3 lysine-9 specific
(4)
Huntingtin yeast partner B
(4)
Huntingtin-interacting protein 1
(4)
Huntingtin-interacting protein B
(4)
Lysine N-methyltransferase 1
(4)
Lysine N-methyltransferase 2A
(4)
Lysine N-methyltransferase 3A
(4)
Lysine-specific methyltransferase 5B
(4)
MLL cleavage product C180
(4)
MLL cleavage product N320
(4)
Myeloid/lymphoid or mixed-lineage leukemia
(4)
Myeloid/lymphoid or mixed-lineage leukemia protein 1
(4)
N-terminal cleavage product of 320 kDa
(4)
PKMT
(4)
Protein lysine methyltransferase clr4
(4)
Protein-lysine N-methyltransferase SETD2
(4)
SET domain-containing protein 2
(4)
Su(var)4-20 homolog 1
(4)
Suppressor of variegation 4-20 homolog 1
(4)
Suv4-20h1
(4)
Trithorax-like protein
(4)
Zinc finger protein HRX
(4)
hSET2
(4)
p180
(4)
p231HBP
(4)
p320
(4)
H3-K9-HMTase 4
(3)
H3-K9-HMTase 6
(3)
Histone H3-K9 methyltransferase 4
(3)
Histone H3-K9 methyltransferase 6
(3)
Histone-lysine N-methyltransferase, H3 lysine-9 specific SUVH4
(3)
 
More...
 
Molecule type  (1)
Protein
(187)
 
Gene names  (128)
KIAA1717
(32)
KMT7
(32)
SET7
(32)
SET9
(32)
SETD7
(32)
SMYD3
(18)
ZMYND1
(18)
ZNFN3A1
(18)
EHMT1
(17)
EUHMTASE1
(17)
GLP
(17)
KIAA1876
(17)
KMT1D
(17)
KMT3C
(17)
SMYD2
(17)
BAT8
(15)
C6orf30
(15)
EHMT2
(15)
G9A
(15)
KMT1C
(15)
NG36
(15)
KMT5A
(13)
PRSET7
(13)
SET07
(13)
SET8
(13)
SETD8
(13)
RBCMT
(7)
ASH1L
(6)
KIAA1420
(6)
KMT2H
(6)
A612L
(5)
ATXR5
(5)
RCOM_1460410
(5)
ALL1
(4)
CXXC7
(4)
HIF1
(4)
HRX
(4)
HSPC069
(4)
HTRX
(4)
HYPB
(4)
KIAA1732
(4)
KMT2A
(4)
KMT3A
(4)
MLL
(4)
MLL1
(4)
SET2
(4)
SETD2
(4)
SPBC428.08c
(4)
TRX1
(4)
clr4
(4)
kmt1
(4)
At2g22740
(3)
At5g13960
(3)
CGI-85
(3)
KMT5B
(3)
KYP
(3)
MAC12.7
(3)
SDG23
(3)
SDG33
(3)
SET23
(3)
SET33
(3)
SUV420H1
(3)
SUVH4
(3)
SUVH6
(3)
T9I22.18
(3)
29E8.110
(2)
EZH2
(2)
HALR
(2)
KIAA1506
(2)
KMT1B
(2)
KMT2C
(2)
KMT6
(2)
KMT8
(2)
MLL3
(2)
NCU04402
(2)
PRDM2
(2)
RIZ
(2)
SUV39H2
(2)
Smyd2
(2)
dim-5
(2)
ALR
(1)
ARA267
(1)
At4g13460
(1)
BLIMP1
(1)
Bop
(1)
Hst1
(1)
KIAA1090
(1)
KIAA1231
(1)
KLLA0F24134g
(1)
KMT2D
(1)
KMT3B
(1)
KMT5C
(1)
Kmt5b
(1)
Kmt5c
(1)
MLL2
(1)
MLL4
(1)
MMSET
(1)
Meisetz
(1)
NSD1
(1)
NSD2
(1)
 
More...
 
Interacting Molecules  (33)
Histone H3.1
(15)
Transcription initiation factor TFIID subunit 10
(14)
Histone H4
(7)
Estrogen receptor
(4)
Cellular tumor antigen p53
(2)
DNA (cytosine-5)-methyltransferase 3A
(2)
Histone H3
(2)
Histone H3.2
(2)
Mitogen-activated protein kinase kinase kinase 2
(2)
Retinoblastoma-binding protein 5
(2)
Set1/Ash2 histone methyltransferase complex subunit ASH2
(2)
B30.2/SPRY domain-containing protein
(1)
DNA (5'-D(*AP*CP*TP*GP*AP*TP*GP*AP*GP*TP*AP*CP*CP*AP*T)-3')
(1)
DNA (5'-D(*AP*CP*TP*GP*CP*TP*GP*AP*GP*TP*AP*CP*CP*AP*T)-3')
(1)
DNA (5'-D(*CP*AP*CP*TP*GP*CP*TP*GP*AP*GP*TP*AP*CP*T)-3')
(1)
DNA (5'-D(*GP*AP*GP*TP*AP*CP*TP*(5CM)P*AP*GP*CP*AP*GP*T)-3')
(1)
DNA (5'-D(*GP*GP*TP*AP*CP*TP*(5CM)P*AP*GP*CP*AP*GP*TP*AP*T)-3')
(1)
DNA (5'-D(*GP*GP*TP*AP*CP*TP*(5CM)P*AP*TP*CP*AP*GP*TP*AP*T)-3')
(1)
DNA 5'-ACTGATGAGTACCAT-3'
(1)
DNA 5'-GGTACT(5CM)ATCAGTAT-3'
(1)
Dnmt1
(1)
H3
(1)
Histone H3.3C
(1)
Mono-Methylated H3K9 Peptide
(1)
Monomethylated p53 peptide
(1)
Protein-lysine N-trimethyltransferase SMYD5
(1)
Sdc1
(1)
Swd1
(1)
Swd3
(1)
UNKNOWN PEPTIDE
(1)
Vascular endothelial growth factor receptor 1
(1)
histone H3.1
(1)
p53 peptide
(1)
 
Interacting ligands  (77)
ZN : ZINC ION
(117)
SAH : S-ADENOSYL-L-HOMOCYSTEINE
(80)
SAM : S-ADENOSYLMETHIONINE
(64)
GOL : GLYCEROL
(24)
EDO : 1,2-ETHANEDIOL
(13)
SO4 : SULFATE ION
(9)
DMS : DIMETHYL SULFOXIDE
(8)
SFG : SINEFUNGIN
(8)
CL : CHLORIDE ION
(7)
BME : BETA-MERCAPTOETHANOL
(6)
BU3 : (R,R)-2,3-BUTANEDIOL
(5)
NA : SODIUM ION
(3)
7KZ : N4-(1-methylpiperidin-4-yl)-N2-hexyl-6,7-dimethoxyquinazoline-2,4-diamine
(2)
7L6 : 6,7-dimethoxy-N-(1-methylpiperidin-4-yl)-2-(morpholin-4-yl)quinazolin-4-amine
(2)
90P : N~2~-cyclohexyl-N~4~-(1-ethylpiperidin-4-yl)-6,7-dimethoxy-N~2~-methylquinazoline-2,4-diamine
(2)
9HG : N~2~-cyclopentyl-6,7-dimethoxy-N~2~-methyl-N~4~-(1-methylpiperidin-4-yl)quinazoline-2,4-diamine
(2)
9HJ : 6,7-dimethoxy-N~2~-methyl-N~4~-(1-methylpiperidin-4-yl)-N~2~-propylquinazoline-2,4-diamine
(2)
ACY : ACETIC ACID
(2)
DIO : 1,4-DIETHYLENE DIOXIDE
(2)
JDG : 2-cyclohexyl-7-methoxy-N-[1-(propan-2-yl)piperidin-4-yl]-8-[3-(pyrrolidin-1-yl)propoxy]-3H-1,4-benzodiazepin-5-amine
(2)
LYS : LYSINE
(2)
MG : MAGNESIUM ION
(2)
MLZ : N-METHYL-LYSINE
(2)
NI : NICKEL (II) ION
(2)
TRS : 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL
(2)
UNL : Unknown ligand
(2)
0N6 : (R)-(3-(3-cyanophenyl)-1-oxo-1-(pyrrolidin-1-yl)propan-2-yl)-1,2,3,4-tetrahydroisoquinoline-6-sulfonamide
(1)
0UM : (2S,5S)-2-amino-6-[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]-5-(propylamino)hexanoic acid
(1)
1L4 : N-[(2R)-3-(3-cyanophenyl)-1-oxo-1-(pyrrolidin-1-yl)propan-2-yl]-8-fluoro-1,2,3,4-tetrahydroisoquinoline-6-sulfonamide
(1)
1L8 : 8-fluoro-N-{(2R)-1-oxo-1-(pyrrolidin-1-yl)-3-[3-(trifluoromethyl)phenyl]propan-2-yl}-1,2,3,4-tetrahydroisoquinoline-6-sulfonamide
(1)
2OD : 5'-methoxy-6'-[3-(pyrrolidin-1-yl)propoxy]spiro[cyclobutane-1,3'-indol]-2'-amine
(1)
3UJ : 5-cyano-2'-{4-[2-(3-methyl-1H-indol-1-yl)ethyl]piperazin-1-yl}-N-[3-(pyrrolidin-1-yl)propyl]biphenyl-3-carboxamide
(1)
4GQ : N-cyclohexyl-N~3~-[2-(3,4-dichlorophenyl)ethyl]-N-(2-{[(2R)-2-hydroxy-2-(3-oxo-3,4-dihydro-2H-1,4-benzoxazin-8-yl)ethyl]amino}ethyl)-beta-alaninamide
(1)
4ZW : 2-oxidanylidene-N-piperidin-4-yl-1,3-dihydroindole-5-carboxamide
(1)
4ZX : 6-chloranyl-2-oxidanylidene-N-[(1S,5R)-8-[4-[(phenylmethyl)amino]piperidin-1-yl]sulfonyl-8-azabicyclo[3.2.1]octan-3-yl]-1,3-dihydroindole-5-carboxamide
(1)
539 : 6,7-dichloro-N-cyclopentyl-4-(pyridin-4-yl)phthalazin-1-amine
(1)
62X : 5'-{[(3S)-3-amino-3-carboxypropyl][3-(dimethylamino)propyl]amino}-5'-deoxyadenosine
(1)
6T1 : 2-[2-[1-[2-(3,4-dichlorophenyl)ethyl]azetidin-3-yl]oxyphenyl]-~{N}-(3-pyrrolidin-1-ylpropyl)pyridine-4-carboxamide
(1)
6TL : 5-[2-[4-[2-(1~{H}-indol-3-yl)ethyl]piperazin-1-yl]phenyl]-~{N}-(3-pyrrolidin-1-ylpropyl)pyridine-3-carboxamide
(1)
6TM : 6-[2-[4-[2-(3,4-dichlorophenyl)ethyl]piperazin-1-yl]phenyl]-~{N}-(3-pyrrolidin-1-ylpropyl)-2~{H}-pyrazolo[3,4-b]pyridine-4-carboxamide
(1)
75P : 7-(2-aminoethoxy)-6-methoxy-2-(pyrrolidin-1-yl)-N-[5-(pyrrolidin-1-yl)pentyl]quinazolin-4-amine
(1)
76K : [(2~{S},5~{R})-1-[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]-5-azaniumyl-6-oxidanyl-6-oxidanylidene-hexan-2-yl]-(3-oxidanylpropyl)azanium
(1)
76O : [(2~{R},5~{S})-1-[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]-5-azaniumyl-6-oxidanyl-6-oxidanylidene-hexan-2-yl]-(phenylmethyl)azanium
(1)
7BY : N-(3-{[6,7-dimethoxy-2-(pyrrolidin-1-yl)quinazolin-4-yl]amino}propyl)propanamide
(1)
8HF : propyl (2~{R})-4-[4-chloranyl-2-[4-(2-oxidanylpropan-2-yl)phenyl]quinolin-7-yl]carbonyl-2-methyl-piperazine-1-carboxylate
(1)
8HR : propyl 4-(4-chloranyl-2-phenyl-quinolin-7-yl)carbonylpiperazine-1-carboxylate
(1)
8NR : ethyl 4-(5,6,7,8-tetrahydroacridin-3-ylcarbonyl)piperazine-1-carboxylate
(1)
8W0 : propyl (3~{S})-4-[[(6~{R})-6-(aminomethyl)-5,6,7,8-tetrahydroacridin-3-yl]carbonyl]-3-methyl-piperazine-1-carboxylate
(1)
8WD : N-{(3-endo)-8-[(trans-4-aminocyclohexyl)sulfonyl]-8-azabicyclo[3.2.1]octan-3-yl}-5-cyclopropyl-1,2-oxazole-3-carboxamide
(1)
9SV : 2-(4-methylpiperazin-1-yl)-3-(phenylsulfanyl)naphthalene-1,4-dione
(1)
9ZY : 2-chloro-5-(4-methyl-6-oxo-3-phenylpyrano[2,3-c]pyrazol-1(6H)-yl)benzoic acid
(1)
A4M : [3-(6-amino-2-methyl-9H-purin-9-yl)azetidin-1-yl]{5-[(4-cycloheptylpiperazin-1-yl)methyl]-1-methyl-1H-pyrazol-3-yl}methanone
(1)
C7H : 4-(dibenzo[1,2-a:2',1'-d][7]annulen-11-ylidene)-1-methyl-piperidine
(1)
C7N : 2-(1-methylpiperidin-4-ylidene)tricyclo[9.4.0.0^{3,8}]pentadeca-1(11),3(8),4,6,9,12,14-heptaen-6-ol
(1)
CIQ : 2-cyclohexyl-6-methoxy-N-[1-(1-methylethyl)piperidin-4-yl]-7-(3-pyrrolidin-1-ylpropoxy)quinazolin-4-amine
(1)
CO : COBALT (II) ION
(1)
DXQ : 7-[3-(dimethylamino)propoxy]-6-methoxy-2-(4-methyl-1,4-diazepan-1-yl)-N-(1-methylpiperidin-4-yl)quinazolin-4-amine
(1)
E11 : N~4~-(1-benzylpiperidin-4-yl)-N~2~-[3-(dimethylamino)propyl]-6,7-dimethoxyquinazoline-2,4-diamine
(1)
E1J : N-(3-{[7-(2-aminoethoxy)-6-methoxy-2-(pyrrolidin-1-yl)quinazolin-4-yl]amino}propyl)prop-2-enamide
(1)
E67 : 7-[(5-aminopentyl)oxy]-N~4~-(1-benzylpiperidin-4-yl)-N~2~-[3-(dimethylamino)propyl]-6-methoxyquinazoline-2,4-diamine
(1)
E72 : 7-[(5-aminopentyl)oxy]-N~4~-[1-(5-aminopentyl)piperidin-4-yl]-N~2~-[3-(dimethylamino)propyl]-6-methoxyquinazoline-2,4-diamine
(1)
EPE : 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID
(1)
H41 : N-[1-(N'-CYANO-N-[3-(DIFLUOROMETHOXY)PHENYL]CARBAMIMIDOYL)-3-(3,4-DICHLOROPHENYL)-4,5-DIHYDRO-1H-PYRAZOL-4-YL]-N-ETHYL-2-HYDROXYACETAMIDE
(1)
I9H : N-[3-(4-CHLOROPHENYL)-1-{N'-CYANO-N-[3-(DIFLUOROMETHOXY)PHENYL]CARBAMIMIDOYL}-4,5-DIHYDRO-1H- PYRAZOL-4-YL]-N-ETHYL-2-HYDROXYACETAMIDE
(1)
K15 : 5'-{[(3S)-3-amino-3-carboxypropyl](hexyl)amino}-5'-deoxyadenosine
(1)
KH3 : 5'-{[(3S)-3-amino-3-carboxypropyl][2-(hexylamino)ethyl]amino}-5'-deoxyadenosine
(1)
M3L : N-TRIMETHYLLYSINE
(1)
MES : 2-(N-MORPHOLINO)-ETHANESULFONIC ACID
(1)
MLI : MALONATE ION
(1)
NH5 : N-cyclohexyl-N~3~-[2-(3,4-dichlorophenyl)ethyl]-N-(2-{[2-(5-hydroxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-8-yl)ethyl]amino}ethyl)-beta-alaninamide
(1)
NM4 : (3S)-1-[2-(5-chloro-2,4-dimethoxyphenyl)imidazo[1,2-a]pyridin-7-yl]-N-[(pyridin-4-yl)methyl]pyrrolidin-3-amine
(1)
PE8 : 3,6,9,12,15,18,21-HEPTAOXATRICOSANE-1,23-DIOL
(1)
PEG : DI(HYDROXYETHYL)ETHER
(1)
Q4A : N-(1-benzylpiperidin-4-yl)-6,7-dimethoxy-2-(4-methyl-1,4-diazepan-1-yl)quinazolin-4-amine
(1)
SA8 : S-5'-AZAMETHIONINE-5'-DEOXYADENOSINE
(1)
SCN : THIOCYANATE ION
(1)
SER : SERINE
(1)
 
Function and Biology
EC number / name  (14)
2.1.1.367 : [Histone H3]-lysine(9) N-methyltransferase
(48)
2.1.1.354 : [Histone H3]-lysine(4) N-trimethyltransferase
(41)
2.1.1.364 : [Histone H3]-lysine(4) N-methyltransferase
(39)
2.1.1.361 : [Histone H4]-lysine(20) N-methyltransferase
(21)
2.1.1.355 : [Histone H3]-lysine(9) N-trimethyltransferase
(12)
2.1.1.359 : [Histone H3]-lysine(36) N-trimethyltransferase
(12)
2.1.1.362 : [Histone H4]-N-methyl-L-lysine(20) N-methyltransferase
(8)
2.1.1.127 : [Ribulose-bisphosphate carboxylase]-lysine N-methyltransferase
(7)
2.1.1.259 : [Fructose-bisphosphate aldolase]-lysine N-methyltransferase
(7)
2.1.1.369 : [Histone H3]-lysine(27) N-methyltransferase
(5)
2.1.1.366 : [Histone H3]-N(6),N(6)-dimethyl-lysine(9) N-methyltransferase
(4)
2.1.1.357 : [Histone H3]-lysine(36) N-dimethyltransferase
(3)
2.1.1.356 : [Histone H3]-lysine(27) N-trimethyltransferase
(2)
2.1.1.43 :
(1)
 
Biological function  (29)
histone methyltransferase activity
(103)
protein-lysine N-methyltransferase activity
(94)
zinc ion binding
(87)
p53 binding
(51)
methyltransferase activity
(45)
metal ion binding
(40)
protein binding
(40)
transferase activity
(40)
histone H3K4 trimethyltransferase activity
(38)
RNA polymerase II complex binding
(37)
histone H3K4 monomethyltransferase activity
(32)
histone H3K36 methyltransferase activity
(23)
histone H4K20 methyltransferase activity
(19)
RNA polymerase II cis-regulatory region sequence-specific DNA binding
(18)
RNA polymerase II intronic transcription regulatory region sequence-specific DNA binding
(18)
histone H3K36 dimethyltransferase activity
(18)
histone H4 methyltransferase activity
(18)
histone H3 methyltransferase activity
(17)
histone H3K9 methyltransferase activity
(17)
lysine N-methyltransferase activity
(17)
[ribulose-bisphosphate carboxylase]-lysine N-methyltransferase activity
(7)
histone H3K37 methyltransferase activity
(6)
identical protein binding
(5)
double-stranded DNA binding
(2)
histone H3K4 methyltransferase activity
(2)
histone H3K9 trimethyltransferase activity
(2)
DNA binding
(1)
DNA-binding transcription repressor activity, RNA polymerase II-specific
(1)
transcription corepressor activity
(1)
 
Biological process  (21)
methylation
(45)
chromatin organization
(37)
regulation of DNA-templated transcription
(32)
chromatin remodeling
(29)
heart development
(20)
negative regulation of cell population proliferation
(19)
negative regulation of transcription by RNA polymerase II
(19)
peptidyl-lysine dimethylation
(19)
peptidyl-lysine monomethylation
(19)
regulation of DNA damage response, signal transduction by p53 class mediator
(19)
cellular response to dexamethasone stimulus
(18)
establishment of protein localization
(18)
myotube cell development
(18)
nucleosome assembly
(18)
positive regulation of transcription by RNA polymerase II
(18)
regulation of signal transduction by p53 class mediator
(17)
peptidyl-lysine methylation
(7)
negative regulation of DNA-templated transcription
(1)
positive regulation of myoblast differentiation
(1)
positive regulation of myotube differentiation
(1)
skeletal muscle cell differentiation
(1)
 
Biological cell component  (6)
nucleus
(98)
cytoplasm
(38)
cytosol
(37)
nucleoplasm
(36)
chromosome
(34)
chloroplast
(7)
 
Compound cofactor class  (1)
S-adenosylmethionine
(7)
 
Sequence and Structure classification
SCOP fold  (3)
beta-clip
(24)
open-sided beta-meander
(11)
RuBisCo LSMT C-terminal, substrate-binding domain
(7)
 
SCOP family  (5)
Histone lysine methyltransferases
(15)
Histone H3 K4-specific methyltransferase SET7/9 N-terminal domain
(11)
RuBisCo LSMT C-terminal, substrate-binding domain
(7)
RuBisCo LSMT catalytic domain
(7)
Viral histone H3 Lysine 27 Methyltransferase
(2)
 
CATH class  (4)
Mainly Beta
(180)
Mainly Alpha
(44)
Special
(18)
Alpha Beta
(8)
 
CATH topology  (9)
Beta-clip-like
(180)
Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
(38)
Histone H3 K4-specific methyltransferase SET7/9 N-terminal domain
(32)
Annexin V; domain 1
(18)
Helix Hairpins
(18)
set domain protein methyltransferase, domain 1
(7)
set domain protein methyltransferase, domain 2
(7)
Arc Repressor Mutant, subunit A
(6)
Double Stranded RNA Binding Domain
(1)
 
Pfam accession / name  (12)
PF00856 : SET
(172)
PF05033 : Pre-SET
(48)
PF01753 : zf-MYND
(38)
PF22648 : SET7_N
(32)
PF17907 : AWS
(12)
PF21549 : PRDM2_PR
(8)
PF02182 : SAD_SRA
(7)
PF09273 : Rubis-subs-bind
(7)
PF02493 : MORN
(3)
PF18264 : preSET_CXC
(2)
PF18445 : zf_PR_Knuckle
(1)
PF21225 : zf-C2H2_5
(1)
 
Experimental Information
Diffraction protocol  (2)
Single wavelength
(177)
MAD
(10)
 
Diffraction radiation source type  (2)
Synchrotron
(169)
Rotating anode
(15)
 
Diffraction source  (50)
APS BEAMLINE 19-ID
(20)
APS BEAMLINE 17-ID
(14)
SSRF BEAMLINE BL17U
(13)
APS BEAMLINE 21-ID-D
(12)
APS BEAMLINE 21-ID-G
(11)
APS BEAMLINE 24-ID-E
(9)
APS BEAMLINE 22-ID
(7)
APS BEAMLINE 22-BM
(6)
CLSI BEAMLINE 08ID-1
(6)
APS BEAMLINE 24-ID-C
(5)
APS BEAMLINE 32-ID
(5)
ESRF BEAMLINE ID29
(5)
APS BEAMLINE 14-BM-C
(4)
APS BEAMLINE 23-ID-B
(4)
APS BEAMLINE 23-ID-D
(4)
ESRF BEAMLINE ID23-1
(4)
RIGAKU FR-E SUPERBRIGHT
(4)
RIGAKU RU200
(4)
APS BEAMLINE 31-ID
(3)
DIAMOND BEAMLINE I03
(3)
NSLS BEAMLINE X29A
(3)
NSLS BEAMLINE X6A
(3)
APS BEAMLINE 21-ID-F
(2)
BESSY BEAMLINE 14.1
(2)
DIAMOND BEAMLINE I02
(2)
ESRF BEAMLINE ID14-4
(2)
NSLS BEAMLINE X25
(2)
PHOTON FACTORY BEAMLINE AR-NW12A
(2)
RIGAKU FR-E DW
(2)
RIGAKU MICROMAX-007 HF
(2)
SSRF BEAMLINE BL19U1
(2)
ALS BEAMLINE 8.2.2
(1)
AUSTRALIAN SYNCHROTRON BEAMLINE MX2
(1)
BSRF BEAMLINE 1W2B
(1)
CHESS BEAMLINE A1
(1)
Cu FINE FOCUS
(1)
DIAMOND BEAMLINE I04
(1)
DIAMOND BEAMLINE I04-1
(1)
ESRF BEAMLINE BM30A
(1)
ESRF BEAMLINE ID14-2
(1)
NSLS BEAMLINE X12C
(1)
NSLS BEAMLINE X26C
(1)
PAL/PLS BEAMLINE 4A
(1)
PAL/PLS BEAMLINE 6B
(1)
PHOTON FACTORY BEAMLINE BL-17A
(1)
RIGAKU
(1)
RIGAKU MICROMAX-007
(1)
SPRING-8 BEAMLINE BL32XU
(1)
SRS BEAMLINE PX14.2
(1)
SSRF BEAMLINE BL17U1
(1)
 
Synchrotron site  (15)
APS
(106)
SSRF
(16)
ESRF
(13)
NSLS
(10)
Diamond
(7)
CLSI
(6)
Photon Factory
(3)
BESSY
(2)
PAL/PLS
(2)
ALS
(1)
Australian Synchrotron
(1)
BSRF
(1)
CHESS
(1)
SPring-8
(1)
SRS
(1)
 
Diffraction detector type  (3)
CCD
(144)
Pixel
(26)
Image plate
(10)
 
Refinement software  (6)
REFMAC
(83)
PHENIX
(47)
CNS
(27)
BUSTER
(25)
BUSTER-TNT
(3)
X-PLOR
(2)
 
NMR
NMR software packages  (8)
ARIA
(3)
NMRPipe
(2)
CNS
(1)
Felix
(1)
NMRView
(1)
X-PLOR
(1)
Xplor-NIH
(1)
XwinNMR
(1)
 
NMR Field Strength
500.0 - 600
(3)
600.0 - 700
(3)
700.0 - 800
(2)
800.0 - 900
(1)
 
Representative Structures
Representative Structures
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Entries 1 to 10 of 187
Entries 1 to 10 of 187
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Structure and Substrate of a Histone H3 Lysine Methyltransferase from Paramecium Bursaria Chlorella Virus 1
Manzur KL, Farooq A, Zeng L, Plotnikova O, Sachchidanand, Koch AW, Zhou M-M
Nat Struct Biol (2003) [PMID: 12567185  ]
Assembly composition: protein only structure
Assembly name: SET domain-containing protein (Preferred)   search this complex
PDBe complex ID: PDB-CPX-128784 (Preferred)   search this ID
PDBe-KB: O41094   
Solution NMR
Released: 28 Jan 2003
Model geometry
Data not deposited
Fit model/data
Data not deposited
1n3j
1n3j
1n3j
Structure of the Neurospora SET domain protein DIM-5, a histone lysine methyltransferase
Zhang X, Tamaru H, Khan SI, Horton JR, Keefe LJ, Selker EU, Cheng X
Cell (2002) [PMID: 12372305  ]
Source organism: Neurospora crassa  
Assembly composition: protein only structure
Bound ligands: ZN    ZN   
Assembly name: Histone-lysine N-methyltransferase, H3 lysine-9 specific dim-5 (Preferred)   search this complex
PDBe complex ID: PDB-CPX-186830 (Preferred)   search this ID
PDBe-KB: Q8X225   
X-ray diffraction
1.98Å resolution
Released: 23 Oct 2002
Model geometry
Fit model/data
Data not deposited
1ml9
1ml9
1ml9
structure of the SET domain histone lysine methyltransferase Clr4
Min JR, Zhang X, Cheng XD, Grewal SIS, Xu R-M
Nat Struct Biol (2002) [PMID: 12389037  ]
Assembly composition: protein only structure
Bound ligands: NI    ZN    NI    SO4    ZN   
Assembly name: Histone-lysine N-methyltransferase, H3 lysine-9 specific (Preferred)   search this complex
PDBe complex ID: PDB-CPX-129896 (Preferred)   search this ID
PDBe-KB: O60016   
X-ray diffraction
2.3Å resolution
Released: 30 Oct 2002
Model geometry
Fit model/data
1mvh
1mvh
1mvh
structure of vSET in complex with meK27 H3 Pept. and cofactor product SAH
Qian CM, Zheng L, Zhou MM
J Mol Biol (2006) [PMID: 16603186  ]
Assembly composition: protein/protein complex
Bound ligands: SAH    SAH   
Modified residues: MLZ    MLZ   
Assembly name: Histone H3 and SET domain-containing protein (Preferred)   search this complex
PDBe complex ID: PDB-CPX-127666 (Preferred)   search this ID
PDBe-KB: O41094    O24165   
Solution NMR
Released: 5 Dec 2006
Model geometry
Fit model/data
Data not analysed
2g46
2g46
2g46
structure of the SET domain histone lysine methyltransferase Clr4
Min JR, Zhang X, Cheng XD, Grewal SIS, Xu R-M
Nat Struct Biol (2002) [PMID: 12389037  ]
Assembly composition: protein only structure
Bound ligands: NI    ZN    NI    SO4    ZN   
Assembly name: Histone-lysine N-methyltransferase, H3 lysine-9 specific (Preferred)   search this complex
PDBe complex ID: PDB-CPX-129896 (Preferred)   search this ID
PDBe-KB: O60016   
X-ray diffraction
3Å resolution
Released: 30 Oct 2002
Model geometry
Fit model/data
1mvx
1mvx
1mvx
Structural basis for the product specificity of histone lysine methyltransferases
Zhang X, Yang Z, Khan SI, Horton JR, Tamaru H, Selker EU, Cheng X
Mol Cell (2003) [PMID: 12887903  ]
Assembly composition: protein/protein complex
Bound ligands: ZN    SAH    ZN    SAH   
Assembly name: Histone-lysine N-methyltransferase, H3 lysine-9 specific dim-5 and Histone H3.1 (Preferred)   search this complex
PDBe complex ID: PDB-CPX-159428 (Preferred)   search this ID
PDBe-KB: Q8X225    P68431   
X-ray diffraction
2.59Å resolution
Released: 5 Aug 2003
Model geometry
Fit model/data
Data not deposited
1peg
1peg
1peg
Structure of G9a SET-domain with Histone H3K9norLeucine mutant peptide and bound S-adenosylmethionine
Jayaram H, Bellon SF, Poy F
Proc Natl Acad Sci U S A (2016) [PMID: 27185940  ]
Source organism: Homo sapiens  
Assembly composition: protein/protein complex
Bound ligands: SAM    SAM    ZN    ZN   
Modified residues: NLE    NLE   
Assembly name: Histone-lysine N-methyltransferase EHMT2 and Histone H3.1 (Preferred)   search this complex
PDBe complex ID: PDB-CPX-159461 (Preferred)   search this ID
PDBe-KB: Q96KQ7    P68431   
X-ray diffraction
1.48Å resolution
Released: 14 Sep 2016
Model geometry
Fit model/data
5jiy
5jiy
5jiy
Structure of G9a SET-domain with Histone H3K9M mutant peptide and bound S-adenosylmethionine
Jayaram H, Bellon SF, Poy F
Proc Natl Acad Sci U S A (2016) [PMID: 27185940  ]
Source organism: Homo sapiens  
Assembly composition: protein/protein complex
Bound ligands: SAM    SAM    ZN    ZN   
Assembly name: Histone-lysine N-methyltransferase EHMT2 and Histone H3.1 (Preferred)   search this complex
PDBe complex ID: PDB-CPX-159461 (Preferred)   search this ID
PDBe-KB: Q96KQ7    P68431   
X-ray diffraction
1.85Å resolution
Released: 6 Jul 2016
Model geometry
Fit model/data
5jin
5jin
5jin
Methyltransferase domain of human suppressor of variegation 3-9 homolog 2 (SUV39H2) in complex with OTS186935 inhibitor
Halabelian L, Dong A, Zeng H, Loppnau P, Bountra C, Edwards AM, Arrowsmith CH, Brown PJ, Structural Genomics Consortium (SGC)
To be published
Source organism: Homo sapiens  
Assembly composition: protein only structure
Bound ligands: ZN    NM4    ZN    NM4   
Assembly name: Histone-lysine N-methyltransferase SUV39H2 (Preferred)   search this complex
PDBe complex ID: PDB-CPX-190624 (Preferred)   search this ID
PDBe-KB: Q9H5I1   
X-ray diffraction
2.4Å resolution
Released: 29 May 2019
Model geometry
Data not analysed
Fit model/data
Data not analysed
6p0r
6p0r
6p0r
Crystal Structure of ATXR5 SET domain in complex with K36me3 histone H3 peptide
Bergamin E, Sarvan S, Malette J, Eram M, Yeung S, Mongeon V, Joshi M, Brunzelle JS, Michaels SD, Blais A, Vedadi M, Couture JF
Nucleic Acids Res (2017) [PMID: 28383693  ]
Assembly composition: protein/protein complex
Bound ligands: DMS    SAH    DMS    SAH   
Assembly name: Probable Histone-lysine N-methyltransferase ATXR5 and Histone H3.2 (Preferred)   search this complex
PDBe complex ID: PDB-CPX-110885 (Preferred)   search this ID
PDBe-KB: B9RU15    Q71DI3   
X-ray diffraction
1.949Å resolution
Released: 19 Apr 2017
Model geometry
Fit model/data
5vac
5vac
5vac
...
Entries 1 to 10 of 187
Entries 1 to 10 of 187