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6GHA

USP15 catalytic domain structure

Functional Information from GO Data
ChainGOidnamespacecontents
A0004843molecular_functioncysteine-type deubiquitinase activity
A0016579biological_processprotein deubiquitination
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN A 1001
ChainResidue
ACYS419
ACYS422
ACYS780
ACYS783

Functional Information from PROSITE/UniProt
site_idPS00972
Number of Residues16
DetailsUSP_1 Ubiquitin specific protease (USP) domain signature 1. GLsnlGNtCFMNSaIQ
ChainResidueDetails
AGLY261-GLN276

site_idPS00973
Number of Residues18
DetailsUSP_2 Ubiquitin specific protease (USP) domain signature 2. YnLiAVsnHyGgmgg..GHY
ChainResidueDetails
ATYR846-TYR863

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU01035, ECO:0000305|PubMed:19553310, ECO:0000305|PubMed:21947082, ECO:0000305|PubMed:22344298, ECO:0000305|PubMed:24852371, ECO:0000305|PubMed:27368102, ECO:0000305|PubMed:33093067
ChainResidueDetails
AASN298

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10092, ECO:0000255|PROSITE-ProRule:PRU10093
ChainResidueDetails
AILE891

224004

PDB entries from 2024-08-21

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