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2VHF

Structure of the CYLD USP domain

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 Residues4
DetailsBINDING SITE FOR RESIDUE ZN A1957
ChainResidue
ACYS788
ACYS791
ACYS817
ACYS820

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A1958
ChainResidue
ACYS799
ACYS802
AHIS825
AHIS833

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B1956
ChainResidue
BCYS791
BCYS817
BCYS820
BCYS788

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B1957
ChainResidue
BCYS799
BCYS802
BHIS825
BHIS833

Functional Information from PROSITE/UniProt
site_idPS00972
Number of Residues16
DetailsUSP_1 Ubiquitin specific protease (USP) domain signature 1. GIqghYNsCYLDStLF
ChainResidueDetails
AGLY593-PHE608

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues104
DetailsRegion: {"description":"B-box","evidences":[{"source":"PubMed","id":"18313383","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27591049","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PROSITE-ProRule","id":"PRU10092","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"18313383","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"18313383","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"18313383","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

238582

PDB entries from 2025-07-09

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