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6F5H

Crystal structure of USP7 in complex with a 4-hydroxypiperidine based inhibitor

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 Residues7
Detailsbinding site for residue SO4 A 1001
ChainResidue
AGLN219
AARG262
AGLY275
ATHR276
ALYS277
ALYS278
AHOH1233

site_idAC2
Number of Residues5
Detailsbinding site for residue GOL A 1002
ChainResidue
ASER341
ALYS391
AHOH1140
ASER330
ATYR331

site_idAC3
Number of Residues15
Detailsbinding site for residue CQ5 A 1003
ChainResidue
ATYR224
AASP295
AVAL296
AGLN297
ALEU406
AMET407
AARG408
APHE409
ALYS420
AHIS456
AASN460
AHIS461
ATYR465
ATYR514
AHOH1159

site_idAC4
Number of Residues8
Detailsbinding site for residue SO4 B 1001
ChainResidue
BGLY275
BTHR276
BLYS277
BLYS278
BHOH1103
BHOH1132
BHOH1154
BHOH1229

site_idAC5
Number of Residues3
Detailsbinding site for residue SO4 B 1002
ChainResidue
BGLY475
BTHR489
BLYS490

site_idAC6
Number of Residues15
Detailsbinding site for residue CQ5 B 1003
ChainResidue
BTYR224
BASP295
BVAL296
BGLN297
BLEU406
BMET407
BARG408
BPHE409
BLYS420
BHIS456
BASN460
BHIS461
BTYR465
BTYR514
BHOH1199

Functional Information from PROSITE/UniProt
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 Residues2
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
BCYS223

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:12507430
ChainResidueDetails
AHIS464
BHIS464

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
BASN218electrostatic stabiliser
BCYS223nucleofuge, nucleophile, proton acceptor, proton donor
BHIS464proton acceptor, proton donor
BASP481electrostatic stabiliser

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PDB entries from 2024-08-21

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