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5QIX

Covalent fragment group deposition -- Crystal Structure of OUTB2 in complex with PCM-0103007

Functional Information from GO Data
ChainGOidnamespacecontents
A0004843molecular_functioncysteine-type deubiquitinase activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0006508biological_processproteolysis
A0008234molecular_functioncysteine-type peptidase activity
A0016579biological_processprotein deubiquitination
A0016787molecular_functionhydrolase activity
A0035871biological_processprotein K11-linked deubiquitination
A0043130molecular_functionubiquitin binding
A0070536biological_processprotein K63-linked deubiquitination
A0071108biological_processprotein K48-linked deubiquitination
A2000780biological_processnegative regulation of double-strand break repair
Functional Information from PDB Data
site_idAC1
Number of Residues9
Detailsbinding site for residue J5V A 301
ChainResidue
AGLY47
AASP48
AARG49
AASN50
ACYS51
AGLU174
ATHR222
ASER223
AHIS224

site_idAC2
Number of Residues4
Detailsbinding site for residue EDO A 302
ChainResidue
APHE6
AASN7
ASER10
ALYS44

site_idAC3
Number of Residues7
Detailsbinding site for residue EDO A 303
ChainResidue
AARG77
APHE142
AGLN185
AALA186
ASER188
AHOH435
AHOH489

site_idAC4
Number of Residues1
Detailsbinding site for residue EDO A 304
ChainResidue
AHIS93

site_idAC5
Number of Residues2
Detailsbinding site for residue EDO A 305
ChainResidue
AASN100
AHOH416

site_idAC6
Number of Residues5
Detailsbinding site for residue EDO A 306
ChainResidue
AARG29
AASN145
AHOH419
AHOH496
AHOH577

site_idAC7
Number of Residues7
Detailsbinding site for residue EDO A 307
ChainResidue
ASER114
ASER116
ASER117
ALYS120
AASP159
AHOH401
AHOH597

site_idAC8
Number of Residues8
Detailsbinding site for residue EDO A 308
ChainResidue
ALEU16
ALEU19
AASN83
AALA87
AHOH406
AHOH438
AHOH519
AHOH571

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000305|PubMed:15258613
ChainResidueDetails
AASP48
AHIS224

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000305|PubMed:12704427, ECO:0000305|PubMed:15258613
ChainResidueDetails
ACYS51

site_idSWS_FT_FI3
Number of Residues1
DetailsSITE: Required to orient and stabilize the active site H-224 => ECO:0000305|PubMed:15258613
ChainResidueDetails
AASN226

223532

PDB entries from 2024-08-07

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