Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

3RIS

Crystal structure of the catalytic domain of UCHL5, a proteasome-associated human deubiquitinating enzyme, reveals an unproductive form of the enzyme

Functional Information from GO Data
ChainGOidnamespacecontents
A0004843molecular_functioncysteine-type deubiquitinase activity
A0006511biological_processubiquitin-dependent protein catabolic process
A0016579biological_processprotein deubiquitination
A0031011cellular_componentIno80 complex
A0070628molecular_functionproteasome binding
B0004843molecular_functioncysteine-type deubiquitinase activity
B0006511biological_processubiquitin-dependent protein catabolic process
B0016579biological_processprotein deubiquitination
B0031011cellular_componentIno80 complex
B0070628molecular_functionproteasome binding
C0004843molecular_functioncysteine-type deubiquitinase activity
C0006511biological_processubiquitin-dependent protein catabolic process
C0016579biological_processprotein deubiquitination
C0031011cellular_componentIno80 complex
C0070628molecular_functionproteasome binding
D0004843molecular_functioncysteine-type deubiquitinase activity
D0006511biological_processubiquitin-dependent protein catabolic process
D0016579biological_processprotein deubiquitination
D0031011cellular_componentIno80 complex
D0070628molecular_functionproteasome binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 241
ChainResidue
AARG137
AGLN138
AHOH252
AHOH291
CGLN146

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 241
ChainResidue
DGLN146
BARG137
BGLN138
BHOH248
BHOH269

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL B 242
ChainResidue
BARG174
BGLY189
BALA190

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 D 241
ChainResidue
BGLN146
DARG137
DGLN138

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Nucleophile => ECO:0000305
ChainResidueDetails
ACYS88
BCYS88
CCYS88
DCYS88

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: Proton donor => ECO:0000250
ChainResidueDetails
AHIS164
BHIS164
CHIS164
DHIS164

site_idSWS_FT_FI3
Number of Residues4
DetailsSITE: Important for enzyme activity => ECO:0000250
ChainResidueDetails
AASP179
BASP179
CASP179
DASP179

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q9WUP7
ChainResidueDetails
ALYS47
BLYS47
CLYS47
DLYS47

site_idSWS_FT_FI5
Number of Residues4
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS158
BLYS158
CLYS158
DLYS158

222415

PDB entries from 2024-07-10

PDB statisticsPDBj update infoContact PDBjnumon