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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

9IML

Sertraline enhances the deubiquitinase activity of USP7 by binding to its switching loop region

Functional Information from GO Data
ChainGOidnamespacecontents
A0004843molecular_functioncysteine-type deubiquitinase activity
A0016579biological_processprotein deubiquitination
C0004843molecular_functioncysteine-type deubiquitinase activity
C0016579biological_processprotein deubiquitination
E0004843molecular_functioncysteine-type deubiquitinase activity
E0016579biological_processprotein deubiquitination
G0004843molecular_functioncysteine-type deubiquitinase activity
G0016579biological_processprotein deubiquitination
Functional Information from PROSITE/UniProt
site_idPS00299
Number of Residues26
DetailsUBIQUITIN_1 Ubiquitin domain signature. KakIqDkegIPpdqQrLIFaGkqleD
ChainResidueDetails
BLYS27-ASP52
site_idPS00972
Number of Residues16
DetailsUSP_1 Ubiquitin specific protease (USP) domain signature 1. GLknqGAtCYMNSlLQ
ChainResidueDetails
AGLY215-GLN230
site_idPS00973
Number of Residues18
DetailsUSP_2 Ubiquitin specific protease (USP) domain signature 2. YiLhAVlvHsGdnhg..GHY
ChainResidueDetails
ATYR448-TYR465
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"12507430","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25944111","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11923872","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"15053880","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"16964248","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"18716620","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"21745816","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"22411829","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues4
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"12507430","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues8
DetailsSite: {"description":"Interacts with activating enzyme"}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues4
DetailsSite: {"description":"Essential for function"}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine; by PINK1","evidences":[{"source":"PubMed","id":"24660806","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24751536","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24784582","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25527291","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues4
DetailsModified residue: {"description":"(Microbial infection) ADP-ribosylthreonine","evidences":[{"source":"PubMed","id":"32330457","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues4
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"16443603","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues8
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"16543144","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18719106","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues8
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"16443603","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16543144","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues4
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"15466860","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues4
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"16543144","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25752573","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25752577","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"34239127","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues4
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"25752577","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
Catalytic Information from CSA
site_idMCSA1
Number of Residues4
DetailsM-CSA 789
ChainResidueDetails
AASN218electrostatic stabiliser
ACYS223nucleofuge, nucleophile, proton acceptor, proton donor
AHIS464proton acceptor, proton donor
AASP481electrostatic stabiliser
site_idMCSA2
Number of Residues4
DetailsM-CSA 789
ChainResidueDetails
CASN218electrostatic stabiliser
CCYS223nucleofuge, nucleophile, proton acceptor, proton donor
CHIS464proton acceptor, proton donor
CASP481electrostatic stabiliser
site_idMCSA3
Number of Residues4
DetailsM-CSA 789
ChainResidueDetails
EASN218electrostatic stabiliser
ECYS223nucleofuge, nucleophile, proton acceptor, proton donor
EHIS464proton acceptor, proton donor
EASP481electrostatic stabiliser
site_idMCSA4
Number of Residues4
DetailsM-CSA 789
ChainResidueDetails
GASN218electrostatic stabiliser
GCYS223nucleofuge, nucleophile, proton acceptor, proton donor
GHIS464proton acceptor, proton donor
GASP481electrostatic stabiliser

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PDB entries from 2026-01-14

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