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5KYC

Crystal structure of USP7 catalytic domain [V302K] mutant in complex with ubiquitin (malonate bound)

Functional Information from GO Data
ChainGOidnamespacecontents
B0004843molecular_functioncysteine-type deubiquitinase activity
B0016579biological_processprotein deubiquitination
Functional Information from PDB Data
site_idAC1
Number of Residues10
Detailsbinding site for residue MLA B 601
ChainResidue
BTYR224
CARG74
BASP295
BVAL296
BPHE409
BTYR514
BHOH719
BHOH761
BHOH765
BHOH903

site_idAC2
Number of Residues6
Detailsbinding site for residue GOL B 602
ChainResidue
BGLN237
BLYS322
BPRO400
BGLU526
BVAL527
BHOH784

site_idAC3
Number of Residues8
Detailsbinding site for residue GOL B 603
ChainResidue
BARG340
BGLU390
BLYS394
BGLU435
BPHE436
BHOH708
BHOH891
BHOH946

Functional Information from PROSITE/UniProt
site_idPS00299
Number of Residues26
DetailsUBIQUITIN_1 Ubiquitin domain signature. KakIqDkegIPpdqQrLIFaGkqleD
ChainResidueDetails
CLYS27-ASP52

site_idPS00972
Number of Residues16
DetailsUSP_1 Ubiquitin specific protease (USP) domain signature 1. GLknqGAtCYMNSlLQ
ChainResidueDetails
BGLY215-GLN230

site_idPS00973
Number of Residues18
DetailsUSP_2 Ubiquitin specific protease (USP) domain signature 2. YiLhAVlvHsGdnhg..GHY
ChainResidueDetails
BTYR448-TYR465

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsSITE: Interacts with activating enzyme
ChainResidueDetails
CARG54
CARG72

site_idSWS_FT_FI2
Number of Residues1
DetailsSITE: Essential for function
ChainResidueDetails
CHIS68

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine; by PINK1 => ECO:0000269|PubMed:24660806, ECO:0000269|PubMed:24751536, ECO:0000269|PubMed:24784582, ECO:0000269|PubMed:25527291
ChainResidueDetails
CSER65

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: (Microbial infection) ADP-ribosylthreonine => ECO:0000269|PubMed:32330457
ChainResidueDetails
CTHR66

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: ADP-ribosylglycine => ECO:0000269|PubMed:28525742
ChainResidueDetails
CGLY76

site_idSWS_FT_FI6
Number of Residues1
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603
ChainResidueDetails
CLYS6

site_idSWS_FT_FI7
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)
ChainResidueDetails
CGLY76

site_idSWS_FT_FI8
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:16543144
ChainResidueDetails
CLYS11
CLYS48

site_idSWS_FT_FI9
Number of Residues1
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000305|PubMed:15466860
ChainResidueDetails
CLYS27

site_idSWS_FT_FI10
Number of Residues1
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
CLYS29

site_idSWS_FT_FI11
Number of Residues1
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:25752577
ChainResidueDetails
CLYS33

site_idSWS_FT_FI12
Number of Residues1
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:18719106
ChainResidueDetails
CLYS63

Catalytic Information from CSA
site_idMCSA1
Number of Residues4
DetailsM-CSA 789
ChainResidueDetails
BPHE234electrostatic stabiliser
BARG239nucleofuge, nucleophile, proton acceptor, proton donor
BPHE480proton acceptor, proton donor
BASN497electrostatic stabiliser

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PDB entries from 2024-07-24

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