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5CHT

Crystal structure of USP18

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 A 401
ChainResidue
ACYS175
ACYS178
ACYS226
ACYS229

site_idAC2
Number of Residues4
Detailsbinding site for residue ZN A 402
ChainResidue
AHIS334
ACYS336
BHIS334
BCYS336

site_idAC3
Number of Residues4
Detailsbinding site for residue ZN B 401
ChainResidue
BCYS178
BCYS226
BCYS229
BCYS175

Functional Information from PROSITE/UniProt
site_idPS00972
Number of Residues16
DetailsUSP_1 Ubiquitin specific protease (USP) domain signature 1. GLhniGQtCCLNSlLQ
ChainResidueDetails
AGLY53-GLN68

site_idPS00973
Number of Residues18
DetailsUSP_2 Ubiquitin specific protease (USP) domain signature 2. YeLfAViaHvGmadf..GHY
ChainResidueDetails
ATYR298-TYR315

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10092, ECO:0000255|PROSITE-ProRule:PRU10093
ChainResidueDetails
ACYS61
BCYS61

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10092, ECO:0000255|PROSITE-ProRule:PRU10093
ChainResidueDetails
AHIS314
BHIS314

223166

PDB entries from 2024-07-31

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