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8BS3

Structure of USP36 in complex with Fubi-PA

Functional Information from GO Data
ChainGOidnamespacecontents
A0004843molecular_functioncysteine-type deubiquitinase activity
A0016579biological_processprotein deubiquitination
Functional Information from PROSITE/UniProt
site_idPS00290
Number of Residues7
DetailsIG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YSCHAGH
ChainResidueDetails
ATYR376-HIS382

site_idPS00299
Number of Residues26
DetailsUBIQUITIN_1 Ubiquitin domain signature. KahVaSlegIApedQvVLLaGapleD
ChainResidueDetails
BLYS25-ASP50

site_idPS00972
Number of Residues16
DetailsUSP_1 Ubiquitin specific protease (USP) domain signature 1. GLhnlGNtCFLNAtIQ
ChainResidueDetails
AGLY123-GLN138

site_idPS00973
Number of Residues19
DetailsUSP_2 Ubiquitin specific protease (USP) domain signature 2. YgLyAVlvHsGyscha.GHY
ChainResidueDetails
ATYR365-TYR383

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10092, ECO:0000255|PROSITE-ProRule:PRU10093, ECO:0000269|PubMed:19208757, ECO:0000269|PubMed:21268071, ECO:0000269|PubMed:25775507, ECO:0000269|PubMed:27445338, ECO:0000269|PubMed:29274341
ChainResidueDetails
ACYS131

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10092, ECO:0000255|PROSITE-ProRule:PRU10093
ChainResidueDetails
AHIS382

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER429

237735

PDB entries from 2025-06-18

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