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6I9C

Structure of the OTU domain of OTULIN G281R mutant

Functional Information from GO Data
ChainGOidnamespacecontents
A0004843molecular_functioncysteine-type deubiquitinase activity
A1990108biological_processprotein linear deubiquitination
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue GOL A 401
ChainResidue
AASP268
AGLY270
AARG274
AGOL402
AHOH533

site_idAC2
Number of Residues5
Detailsbinding site for residue GOL A 402
ChainResidue
AHOH606
ATYR165
ATRP167
AASN245
AGOL401

site_idAC3
Number of Residues6
Detailsbinding site for residue GOL A 403
ChainResidue
AGLU95
ATRP96
AARG97
ALYS116
AGLN303
ATHR331

site_idAC4
Number of Residues6
Detailsbinding site for residue GOL A 404
ChainResidue
AASN127
ALYS233
AHIS276
ALEU277
AGLN279
AHOH605

site_idAC5
Number of Residues3
Detailsbinding site for residue CL A 405
ChainResidue
ALYS94
AVAL318
AHOH565

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:23708998, ECO:0000269|PubMed:23746843, ECO:0007744|PDB:3ZNZ, ECO:0007744|PDB:4KSL
ChainResidueDetails
AASP126
AHIS339

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:23708998, ECO:0000269|PubMed:23746843, ECO:0000269|PubMed:24726327, ECO:0007744|PDB:3ZNZ, ECO:0007744|PDB:4KSL
ChainResidueDetails
ACYS129

site_idSWS_FT_FI3
Number of Residues1
DetailsSITE: Linear diubiquitin binding => ECO:0000269|PubMed:23708998, ECO:0000269|PubMed:23746843, ECO:0007744|PDB:3ZNZ, ECO:0007744|PDB:4KSK, ECO:0007744|PDB:4KSL
ChainResidueDetails
AGLU314

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PDB entries from 2024-07-24

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