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9IML

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

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
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:12507430, ECO:0000269|PubMed:25944111, ECO:0000305|PubMed:11923872, ECO:0000305|PubMed:15053880, ECO:0000305|PubMed:16964248, ECO:0000305|PubMed:18716620, ECO:0000305|PubMed:21745816, ECO:0000305|PubMed:22411829
ChainResidueDetails
ACYS223
CCYS223
ECYS223
GCYS223
FARG54
FARG72
HARG54
HARG72

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:12507430
ChainResidueDetails
AHIS464
CHIS464
EHIS464
GHIS464

site_idSWS_FT_FI3
Number of Residues4
DetailsMOD_RES: Phosphoserine; by PINK1 => ECO:0000269|PubMed:24660806, ECO:0000269|PubMed:24751536, ECO:0000269|PubMed:24784582, ECO:0000269|PubMed:25527291
ChainResidueDetails
BSER65
DSER65
FSER65
HSER65

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: (Microbial infection) ADP-ribosylthreonine => ECO:0000269|PubMed:32330457
ChainResidueDetails
BTHR66
DTHR66
FTHR66
HTHR66

site_idSWS_FT_FI5
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603
ChainResidueDetails
BLYS6
DLYS6
FLYS6
HLYS6

site_idSWS_FT_FI6
Number of Residues8
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:18719106
ChainResidueDetails
BLYS63
DLYS63
FLYS63
HLYS63

site_idSWS_FT_FI7
Number of Residues8
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:16543144
ChainResidueDetails
BLYS11
BLYS48
DLYS11
DLYS48
FLYS11
FLYS48
HLYS11
HLYS48

site_idSWS_FT_FI8
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000305|PubMed:15466860
ChainResidueDetails
BLYS27
DLYS27
FLYS27
HLYS27

site_idSWS_FT_FI9
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:25752573, ECO:0000269|PubMed:25752577, ECO:0000269|PubMed:34239127
ChainResidueDetails
BLYS29
DLYS29
FLYS29
HLYS29

site_idSWS_FT_FI10
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:25752577
ChainResidueDetails
BLYS33
DLYS33
FLYS33
HLYS33

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 2025-06-18

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