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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
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
BASN298

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10092, ECO:0000255|PROSITE-ProRule:PRU10093
ChainResidueDetails
AILE891
BILE891

222624

PDB entries from 2024-07-17

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