Entry status  (1)

REL

(19)

Experimental methods  (1)

X-ray diffraction

(19)

Authors  (97)

Lauritzen C

(7)

Pedersen J

(7)

Bodnarchuk MS

(5)

Doyle K

(5)

Hughes SJ

(5)

Kack H

(5)

Käck H

(5)

Lonn H

(5)

Lönn H

(5)

Palmer N

(5)

Van De Poel A

(5)

Van De Poël A

(5)

Austin R

(4)

Barber S

(4)

Beri R

(4)

Breed J

(4)

Cage P

(4)

Chohan K

(4)

Debreczeni J

(4)

Edman K

(4)

Ford R

(4)

Furber M

(4)

Gardiner P

(4)

Harper S

(4)

Hutchinson R

(4)

Kinchin E

(4)

Luckhurst C

(4)

Mather A

(4)

Mete A

(4)

Mete T

(4)

Millichip I

(4)

Oreffo V

(4)

Sanganee H

(4)

Sanghanee H

(4)

Stein L

(4)

Thong B

(4)

Tiden A

(4)

Tiden AK

(4)

Wallace A

(4)

Wissler L

(4)

Gauthier F

(3)

Gieldon A

(3)

Hakansson M

(3)

Håkansson M

(3)

Jenne D

(3)

Jenne DE

(3)

Korkmaz B

(3)

Larsen S

(3)

Lesner A

(3)

Logan DT

(3)

Nevins N

(3)

Wysocka M

(3)

Zhao B

(3)

Arnau J

(2)

Concha N

(2)

Cui G

(2)

Dahl SW

(2)

Meek TD

(2)

Molgaard A

(2)

Mølgaard A

(2)

Petersen G

(2)

Rubach JK

(2)

Schneck JL

(2)

Smallwood A

(2)

Taylor AN

(2)

Thrall SH

(2)

Wisnoski D

(2)

Bettoun D

(1)

Davis AB

(1)

Davis R

(1)

Delhom I

(1)

Deng J

(1)

Janjic V

(1)

Janjić V

(1)

Jolit A

(1)

Kadziola A

(1)

Kmett C

(1)

Laine D

(1)

Lainé D

(1)

Lamba D

(1)

Lin G

(1)

McCleland B

(1)

McDevitt P

(1)

Midgett R

(1)

Olsen JG

(1)

Palovich M

(1)

Peck B

(1)

Petitjean E

(1)

Podobnik M

(1)

Schneck J

(1)

Stern I

(1)

Turk B

(1)

Turk D

(1)

Turk V

(1)

Umbrecht S

(1)

Villa J

(1)

Xie H

(1)

Homo / hetero assembly  (2)

hetero

(17)

homo

(2)

Assembly composition  (2)

protein/protein complex

(17)

protein structure

(2)

Assembly polymer count  (5)

trimer

(8)

dodecamer

(6)

tetramer

(3)

dimer

(1)

hexamer

(1)

Resolution distribution

1.0 - 1.5

(1)

1.5 - 2

(10)

2.0 - 2.5

(8)

Release year distribution

2000 - 2005

(2)

2005 - 2010

(2)

2010 - 2015

(7)

2015 - 2020

(10)

Journal  (7)

ACS Med Chem Lett

(6)

J Med Chem

(4)

Biochem Pharmacol

(3)

Biochem J

(2)

Biochemistry

(2)

EMBO J

(1)

FEBS Lett

(1)

Organism superkingdom  (1)

Eukaryota

(19)

Organism name  (2)

Homo sapiens

(18)

Rattus norvegicus

(1)

Molecule name  (13)

Cathepsin C

(19)

Cathepsin J

(19)

DPP-I

(19)

DPPI

(19)

Dipeptidyl peptidase 1

(19)

Dipeptidyl peptidase 1 exclusion domain chain

(19)

Dipeptidyl peptidase 1 heavy chain

(19)

Dipeptidyl peptidase 1 light chain

(19)

Dipeptidyl peptidase I

(19)

Dipeptidyl peptidase I exclusion domain chain

(19)

Dipeptidyl peptidase I heavy chain

(19)

Dipeptidyl peptidase I light chain

(19)

Dipeptidyl transferase

(19)

Molecule type  (1)

Protein

(19)

Gene names  (3)

CPPI

(18)

CTSC

(18)

Ctsc

(1)

Interacting Molecules  (3)

Dipeptidyl peptidase 1 heavy chain

(17)

Dipeptidyl peptidase 1 light chain

(17)

Dipeptidyl peptidase 1 exclusion domain chain

(15)

Interacting ligands  (29)

NAG : 2-acetamido-2-deoxy-beta-D-glucopyranose

(19)

CL : CHLORIDE ION

(18)

BMA : beta-D-mannopyranose

(4)

DMS : DIMETHYL SULFOXIDE

(4)

SO4 : SULFATE ION

(4)

ACT : ACETATE ION

(3)

GOL : GLYCEROL

(3)

MAN : alpha-D-mannopyranose

(3)

1ZB : N-[(1S)-1-benzyl-3-diazen-1-iumylidene-2-oxopropyl]glycinamide

(1)

6AO : (2S)-2-azanyl-N-[(2S)-1-azanylidene-3-(4-phenylphenyl)propan-2-yl]butanamide

(1)

ACY : ACETIC ACID

(1)

EDO : 1,2-ETHANEDIOL

(1)

GDI : (2S)-N-[(2S)-1-AZANYLIDENE-3-[4-(4-CYANOPHENYL)PHENYL]PROPAN-2-YL]PIPERIDINE-2-CARBOXAMIDE

(1)

GLY : GLYCINE

(1)

H9B : (2~{S})-~{N}-[(1~{R},2~{R})-1-(aminomethyl)-2-[4-[4-(trifluoromethyl)phenyl]phenyl]cyclopropyl]-2-azanyl-butanamide

(1)

H9H : 1-azanyl-~{N}-[(1~{R},2~{R})-1-cyano-2-[4-[4-(4-methylpiperazin-1-yl)sulfonylphenyl]phenyl]cyclopropyl]cyclohexane-1-carboxamide

(1)

HB5 : (2~{S})-2-azanyl-~{N}-[(1~{R},2~{R})-1-(iminomethyl)-2-[4-[4-(4-methylpiperazin-1-yl)sulfonylphenyl]phenyl]cyclopropyl]-3-thiophen-2-yl-propanamide

(1)

K9Q : (2~{S},4~{R})-~{N}-[(2~{S})-1-azanyl-3-(4-phenylphenyl)propan-2-yl]-4-oxidanyl-pyrrolidine-2-carboxamide

(1)

K9W : (2~{S})-~{N}-[(2~{S})-1-azanyl-3-[4-(4-cyanophenyl)phenyl]propan-2-yl]pyrrolidine-2-carboxamide

(1)

K9Z : (2~{S},4~{S})-~{N}-[(2~{S})-1-azanyl-3-[4-(4-cyanophenyl)phenyl]propan-2-yl]-4-oxidanyl-pyrrolidine-2-carboxamide

(1)

KA8 : (2~{S},4~{S})-~{N}-[(2~{S})-1-azanyl-3-[4-(4-cyanophenyl)phenyl]propan-2-yl]-4-fluoranyl-pyrrolidine-2-carboxamide

(1)

KAQ : (2~{S},4~{S})-~{N}-[(2~{S})-1-azanyl-3-[4-(4-cyanophenyl)phenyl]propan-2-yl]-4-methylsulfanyl-pyrrolidine-2-carboxamide

(1)

LXV : 2,5-dibromo-N-{(3R,5S)-1-[(Z)-iminomethyl]-5-methylpyrrolidin-3-yl}benzenesulfonamide

(1)

LYS : LYSINE

(1)

PEG : DI(HYDROXYETHYL)ETHER

(1)

SER : SERINE

(1)

TYR : TYROSINE

(1)

U6B : 4-AZANYL-N-[(2S)-1-AZANYLIDENE-3-[4-(4-CYANOPHENYL)PHENYL]PROPAN-2-YL]OXANE-4-CARBOXAMIDE

(1)

W2C : (2S,4S)-N-[(2S)-1-azanylidene-3-[4-(4-cyanophenyl)phenyl]propan-2-yl]-4-oxidanyl-piperidine-2-carboxamide

(1)

EC number / name  (1)

3.4.14.1 : Dipeptidyl-peptidase I

(19)

Biological function  (12)

cysteine-type peptidase activity

(19)

chloride ion binding

(2)

cysteine-type endopeptidase activity

(2)

dipeptidyl-peptidase activity

(2)

hydrolase activity

(2)

identical protein binding

(2)

peptidase activator activity involved in apoptotic process

(2)

peptidase activity

(2)

phosphatase binding

(2)

protein-folding chaperone binding

(2)

serine-type endopeptidase activity

(2)

protein binding

(1)

Biological process  (9)

proteolysis

(19)

T cell mediated cytotoxicity

(2)

apoptotic process

(2)

negative regulation of myelination

(2)

positive regulation of apoptotic signaling pathway

(2)

positive regulation of microglial cell activation

(2)

positive regulation of proteolysis involved in protein catabolic process

(2)

proteolysis involved in protein catabolic process

(2)

immune response

(1)

Biological cell component  (14)

centrosome

(2)

cytoplasm

(2)

extracellular space

(2)

intracellular membrane-bounded organelle

(2)

lysosome

(2)

nucleoplasm

(2)

COPII-coated ER to Golgi transport vesicle

(1)

azurophil granule lumen

(1)

collagen-containing extracellular matrix

(1)

endoplasmic reticulum lumen

(1)

endoplasmic reticulum-Golgi intermediate compartment membrane

(1)

extracellular exosome

(1)

extracellular region

(1)

membrane

(1)

SCOP fold  (2)

Streptavidin-like

(4)

Cysteine proteinases

(2)

SCOP family  (2)

Dipeptidyl peptidase I (cathepsin C), exclusion domain

(4)

Papain-like

(2)

CATH class  (2)

Alpha Beta

(14)

Mainly Beta

(14)

CATH topology  (3)

Cathepsin B; Chain A

(14)

Lipocalin

(14)

OB fold (Dihydrolipoamide Acetyltransferase, E2P)

(12)

Pfam accession / name  (2)

PF00112 : Peptidase_C1

(19)

PF08773 : CathepsinC_exc

(19)

Diffraction protocol  (1)

Single wavelength

(19)

Diffraction radiation source type  (2)

Synchrotron

(12)

Rotating anode

(7)

Diffraction source  (11)

RIGAKU FR-E

(4)

ESRF

(3)

APS BEAMLINE 21-ID-D

(2)

BRUKER X8 PROTEUM

(2)

MAX II BEAMLINE I711

(2)

APS BEAMLINE 21-ID-G

(1)

ELETTRA BEAMLINE 5.2R

(1)

ESRF BEAMLINE ID23-1

(1)

ESRF BEAMLINE ID23-2

(1)

MAX II BEAMLINE I911-2

(1)

RIGAKU RU300

(1)

Synchrotron site  (4)

ESRF

(5)

APS

(3)

MAX II

(3)

ELETTRA

(1)

Diffraction detector type  (3)

CCD

(15)

Image plate

(2)

Area detector

(1)

Refinement software  (5)

REFMAC

(10)

BUSTER

(7)

BUSTER-TNT

(2)

CNS

(2)

MAIN

(1)

Representative Structures

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