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5VSB

Structure of DUB complex

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 Residues13
Detailsbinding site for residue 9QA A 4000
ChainResidue
ATYR224
AHIS456
AHIS461
ATYR465
ATYR514
AASP295
AVAL296
AGLN297
ALEU406
AMET407
AARG408
APHE409
ALYS420

site_idAC2
Number of Residues13
Detailsbinding site for residue 9QA B 4000
ChainResidue
BTYR224
BMET292
BASP295
BVAL296
BGLN297
BLEU406
BMET407
BARG408
BPHE409
BMET410
BHIS456
BTYR465
BTYR514

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
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 Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"12507430","evidenceCode":"ECO:0000305"}]}
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
BASN218electrostatic stabiliser
BCYS223nucleofuge, nucleophile, proton acceptor, proton donor
BHIS464proton acceptor, proton donor
BASP481electrostatic stabiliser

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PDB entries from 2025-07-23

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