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6GH9

USP15 catalytic domain in complex with small molecule

Functional Information from GO Data
ChainGOidnamespacecontents
A0004843molecular_functioncysteine-type deubiquitinase activity
A0016579biological_processprotein deubiquitination
B0004843molecular_functioncysteine-type deubiquitinase activity
B0016579biological_processprotein deubiquitination
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN A 1001
ChainResidue
ACYS419
ACYS422
ACYS780
ACYS783

site_idAC2
Number of Residues2
Detailsbinding site for residue DMS A 1002
ChainResidue
AASP300
AARG371

site_idAC3
Number of Residues5
Detailsbinding site for residue MIX A 1003
ChainResidue
AHIS862
AASP879
AASN264
ATYR855
AGLY856

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 Residues2
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PROSITE-ProRule","id":"PRU01035","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"19553310","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"21947082","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"22344298","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"24852371","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"27368102","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"33093067","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10092","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10093","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

238582

PDB entries from 2025-07-09

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