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6CRN

Structure of the USP15 deubiquitinase domain in complex with a high-affinity first-generation Ubv

Functional Information from GO Data
ChainGOidnamespacecontents
A0004843molecular_functioncysteine-type deubiquitinase activity
A0016579biological_processprotein deubiquitination
B0004843molecular_functioncysteine-type deubiquitinase activity
B0016579biological_processprotein deubiquitination
C0004843molecular_functioncysteine-type deubiquitinase activity
C0016579biological_processprotein deubiquitination
D0004843molecular_functioncysteine-type deubiquitinase activity
D0016579biological_processprotein deubiquitination
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN A 700
ChainResidue
ACYS448
ACYS451
ACYS499
ACYS502

site_idAC2
Number of Residues4
Detailsbinding site for residue ZN B 701
ChainResidue
BCYS448
BCYS451
BCYS499
BCYS502

site_idAC3
Number of Residues4
Detailsbinding site for residue ZN C 701
ChainResidue
CCYS451
CCYS499
CCYS502
CCYS448

site_idAC4
Number of Residues4
Detailsbinding site for residue ZN D 701
ChainResidue
DCYS448
DCYS451
DCYS499
DCYS502

Functional Information from PROSITE/UniProt
site_idPS00972
Number of Residues16
DetailsUSP_1 Ubiquitin specific protease (USP) domain signature 1. GLsnlGNtCFMNSaIQ
ChainResidueDetails
AGLY290-GLN305

site_idPS00973
Number of Residues18
DetailsUSP_2 Ubiquitin specific protease (USP) domain signature 2. YnLiAVsnHyGgmgg..GHY
ChainResidueDetails
ATYR565-TYR582

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
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
ACYS298
BCYS298
CCYS298
DCYS298

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10092, ECO:0000255|PROSITE-ProRule:PRU10093
ChainResidueDetails
AHIS581
BHIS581
CHIS581
DHIS581

site_idSWS_FT_FI3
Number of Residues4
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q8R5H1
ChainResidueDetails
AVAL602
BVAL602
CVAL602
DVAL602

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PDB entries from 2025-07-02

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