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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 Residues2
DetailsACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10092, ECO:0000269|PubMed:18313383
ChainResidueDetails
ACYS601
BCYS601

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:18313383
ChainResidueDetails
AHIS871
BHIS871

site_idSWS_FT_FI3
Number of Residues16
DetailsBINDING: BINDING => ECO:0000269|PubMed:18313383
ChainResidueDetails
ACYS788
BCYS791
BCYS799
BCYS802
BCYS817
BCYS820
BHIS825
BHIS833
ACYS791
ACYS799
ACYS802
ACYS817
ACYS820
AHIS825
AHIS833
BCYS788

219140

PDB entries from 2024-05-01

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