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5QIQ

Covalent fragment group deposition -- Crystal Structure of OUTB2 in complex with PCM-0103050

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 Residues4
Detailsbinding site for residue PEG A 401
ChainResidue
AASP129
AHIS130
AHOH547
AHOH566

site_idAC2
Number of Residues8
Detailsbinding site for residue J5A A 402
ChainResidue
ATHR222
ASER223
AHIS224
AASP48
AARG49
AASN50
ACYS51
APHE52

site_idAC3
Number of Residues7
Detailsbinding site for residue EDO A 403
ChainResidue
APHE6
AASN7
ALEU8
ASER10
ALYS44
ATHR45
ALYS46

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

219140

PDB entries from 2024-05-01

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