Uniprot accession / id : Q9JKB1  OR   Uniprot accession / id : P15374
 
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Entry Information
Entry status  (1)
REL
(5)
 
Experimental methods  (1)
X-ray diffraction
(5)
 
Authors  (48)
Ovaa H
(2)
Chen C
(1)
Chen J
(1)
Cook WJ
(1)
Ding S
(1)
Fish A
(1)
Fu Q
(1)
Galardy PJ
(1)
Gao S
(1)
Gaudet R
(1)
Hill CP
(1)
Hong D
(1)
Jiang Y
(1)
Johnston SC
(1)
Kou X
(1)
Larsen CN
(1)
Liang L
(1)
Liu L
(1)
Mao Z
(1)
Mao ZY
(1)
Meester WJ
(1)
Meester WJN
(1)
Mei Z
(1)
Misaghi S
(1)
Murachelli AG
(1)
Pan M
(1)
Ploegh HL
(1)
Qu Q
(1)
Ren Y
(1)
Sixma TK
(1)
Song Z
(1)
Sun X
(1)
Tang H
(1)
Wang H
(1)
Wang M
(1)
Wang T
(1)
Wilkinson KD
(1)
Xu X
(1)
Xu XJ
(1)
Yang G
(1)
Yang J
(1)
Zhang L
(1)
Zhang Q
(1)
Zhang W
(1)
Zhang WT
(1)
Zheng Q
(1)
van Tilburg GBA
(1)
van der Heden van Noort GJ
(1)
 
Homo / hetero assembly  (2)
hetero
(3)
homo
(2)
 
Assembly composition  (2)
protein/protein complex
(3)
protein structure
(2)
 
Assembly polymer count  (3)
monomer
(2)
trimer
(2)
dimer
(1)
 
Resolution distribution
1.0 - 1.5
(1)
1.5 - 2
(3)
2.0 - 2.5
(1)
 
Release year distribution
1995 - 2000
(1)
2000 - 2005
(1)
2015 - 2020
(2)
2020 - 2025
(2)
 
Journal  (5)
Angew Chem Int Ed Engl
(1)
Cell Chem Biol
(1)
EMBO J
(1)
J Biol Chem
(1)
Nat Commun
(1)
 
Macromolecules
Organism superkingdom  (1)
Eukaryota
(5)
 
Organism name  (1)
Homo sapiens
(5)
 
Molecule name  (3)
UCH-L3
(5)
Ubiquitin carboxyl-terminal hydrolase isozyme L3
(5)
Ubiquitin thioesterase L3
(5)
 
Molecule type  (1)
Protein
(5)
 
Gene names  (1)
UCHL3
(5)
 
Interacting Molecules  (1)
Ubiquitin
(3)
 
Interacting ligands  (6)
CL : CHLORIDE ION
(1)
EDO : 1,2-ETHANEDIOL
(1)
GVE : METHYL 4-AMINOBUTANOATE
(1)
JXY : (2~{S})-2-(4-hydroxyphenyl)-6,8-dimethyl-5,7-bis(oxidanyl)-2,3-dihydrochromen-4-one
(1)
K : POTASSIUM ION
(1)
MG : MAGNESIUM ION
(1)
 
Function and Biology
EC number / name  (1)
3.4.19.12 : Ubiquitinyl hydrolase 1
(5)
 
Biological function  (7)
cysteine-type deubiquitinase activity
(5)
cysteine-type peptidase activity
(5)
deNEDDylase activity
(5)
hydrolase activity
(5)
peptidase activity
(5)
protein binding
(5)
ubiquitin binding
(5)
 
Biological process  (6)
post-translational protein modification
(5)
protein catabolic process
(5)
protein deubiquitination
(5)
protein ubiquitination
(5)
proteolysis
(5)
ubiquitin-dependent protein catabolic process
(5)
 
Biological cell component  (4)
Golgi apparatus
(5)
cytoplasm
(5)
cytosol
(5)
nucleoplasm
(5)
 
Sequence and Structure classification
SCOP fold  (1)
Cysteine proteinases
(2)
 
SCOP family  (1)
Ubiquitin carboxyl-terminal hydrolase UCH-L
(2)
 
CATH class  (1)
Alpha Beta
(3)
 
CATH topology  (1)
Ubiquitin C-terminal Hydrolase UCH-l3
(3)
 
Pfam accession / name  (1)
PF01088 : Peptidase_C12
(5)
 
Experimental Information
Diffraction protocol  (1)
Single wavelength
(4)
 
Diffraction radiation source type  (1)
Synchrotron
(5)
 
Diffraction source  (5)
APS BEAMLINE 8-BM
(1)
ESRF BEAMLINE MASSIF-1
(1)
SSRF BEAMLINE BL02U1
(1)
SSRF BEAMLINE BL17B1
(1)
SSRL BEAMLINE BL7-1
(1)
 
Synchrotron site  (4)
SSRF
(2)
APS
(1)
ESRF
(1)
SSRL
(1)
 
Diffraction detector type  (3)
CCD
(2)
Pixel
(2)
Image plate
(1)
 
Refinement software  (4)
PHENIX
(2)
CNS
(1)
REFMAC
(1)
X-PLOR
(1)
 
Representative Structures
Representative Structures
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Entries 1 to 5 of 5
Entries 1 to 5 of 5
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UCHL3 in complex with synthetic, K27-linked diubiquitin
Murachelli AG, Sixma TK
Cell Chem Biol (2021) [PMID: 33238157  ]
Source organism: Homo sapiens  
Assembly composition: protein/protein complex
Bound ligands: BR    K    K    CL    EDO   
Modified residues: NLE    NLE   
Assembly name: Ubiquitin carboxyl-terminal hydrolase isozyme L3 and Ubiquitin (Preferred)   search this complex
PDBe complex ID: PDB-CPX-143244 (Preferred)   search this ID
PDBe-KB: P15374    P0CG47    P0CG48   
X-ray diffraction
2.1Å resolution
Released: 26 Feb 2020
Model geometry
Fit model/data
6qml
6qml
6qml
Crystal structure of human UCHL3 in complex with Farrerol
Mao ZY, Xu XJ, Zhang WT
Nat Commun (2023) [PMID: 37012254  ]
Source organism: Homo sapiens  
Assembly composition: protein only structure
Bound ligands: JXY   
Assembly name: Ubiquitin carboxyl-terminal hydrolase isozyme L3 (Preferred)   search this complex
PDBe complex ID: PDB-CPX-147331 (Preferred)   search this ID
PDBe-KB: P15374   
X-ray diffraction
1.58Å resolution
Released: 19 Apr 2023
Model geometry
Fit model/data
7yv4
7yv4
7yv4
Crystal structure of UCHL3-UbVME complex
Misaghi S, Galardy PJ, Meester WJN, Ovaa H, Ploegh HL, Gaudet R
J Biol Chem (2005) [PMID: 15531586  ]
Source organism: Homo sapiens  
Assembly composition: protein/protein complex
Bound ligands: MG    GVE    MG    GVE   
Assembly name: Ubiquitin carboxyl-terminal hydrolase isozyme L3 and Ubiquitin (Preferred)   search this complex
PDBe complex ID: PDB-CPX-143340 (Preferred)   search this ID
PDBe-KB: P15374    P0CG48   
X-ray diffraction
1.45Å resolution
Released: 23 Nov 2004
Model geometry
Fit model/data
1xd3
1xd3
1xd3
Crystal structure of Lys27-linked di-ubiquitin in complex with its selective interacting protein UCHL3
Ding S, Pan M, Zheng Q, Ren Y, Hong D
Angew Chem Int Ed Engl (2019) [PMID: 30589182  ]
Source organism: Homo sapiens  
Assembly composition: protein/protein complex
Modified residues: SLZ    SLZ   
Assembly name: Ubiquitin carboxyl-terminal hydrolase isozyme L3 and Ubiquitin (Preferred)   search this complex
PDBe complex ID: PDB-CPX-143235 (Preferred)   search this ID
PDBe-KB: P15374    P0CG47   
X-ray diffraction
1.866Å resolution
Released: 6 Feb 2019
Model geometry
Fit model/data
6isu
6isu
6isu
DEUBIQUITINATING ENZYME UCH-L3 (HUMAN) AT 1.8 ANGSTROM RESOLUTION
Johnston SC, Larsen CN, Cook WJ, Wilkinson KD, Hill CP
EMBO J (1997) [PMID: 9233788  ]
Source organism: Homo sapiens  
Assembly composition: protein only structure
Assembly name: Ubiquitin carboxyl-terminal hydrolase isozyme L3 (Preferred)   search this complex
PDBe complex ID: PDB-CPX-147331 (Preferred)   search this ID
PDBe-KB: P15374   
X-ray diffraction
1.8Å resolution
Released: 28 Jan 1998
Model geometry
Fit model/data
1uch
1uch
1uch
Entries 1 to 5 of 5
Entries 1 to 5 of 5