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3TB3

Crystal structure of the UCH domain of UCH-L5 with 6 residues deleted

Replaces:  3SQA
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 Residues5
DetailsBINDING SITE FOR RESIDUE CA B 228
ChainResidue
AGLU109
AGLU113
BGLU113
BHOH247
BHOH248

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CA B 229
ChainResidue
BGLU109
BGLU113

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000305
ChainResidueDetails
AALA88
BALA88

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 2024-07-24

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