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3RII

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
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 229
ChainResidue
APHE56
ALYS57
ATRP58
AGLN59
AGLU62
ATYR211
AHOH288

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG A 230
ChainResidue
AHOH349
BHOH351
AGLU109
AGLU113

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO B 229
ChainResidue
BALA80
BGLN91
BALA92
BSER95
BGLY180
BHOH335

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000305
ChainResidueDetails
ASER88
BSER88

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000250
ChainResidueDetails
AHIS164
BHIS164

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Important for enzyme activity => ECO:0000250
ChainResidueDetails
AASP179
BASP179

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q9WUP7
ChainResidueDetails
ALYS47
BLYS47

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS158
BLYS158

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PDB entries from 2024-07-10

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