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5QIP

Covalent fragment group deposition -- Crystal Structure of OUTB2 in complex with PCM-0102153

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 J51 A 301
ChainResidue
AGLY47
AASP48
AARG49
AASN50
ACYS51
ATHR222
ASER223
AHOH521
AHOH552

site_idAC2
Number of Residues2
Detailsbinding site for residue EDO A 302
ChainResidue
AARG38
AGLN192

site_idAC3
Number of Residues5
Detailsbinding site for residue EDO A 303
ChainResidue
APHE6
AASN7
ALEU8
ALYS44
ALYS46

site_idAC4
Number of Residues6
Detailsbinding site for residue PEG A 304
ChainResidue
AASP129
AHIS130
AMET171
AHOH403
AHOH404
AHOH484

site_idAC5
Number of Residues2
Detailsbinding site for residue EDO A 305
ChainResidue
AGLY89
AARG144

site_idAC6
Number of Residues2
Detailsbinding site for residue EDO A 306
ChainResidue
AALA202
AASN204

site_idAC7
Number of Residues5
Detailsbinding site for residue EDO A 307
ChainResidue
AASP176
AHIS177
AILE180
ATYR195
ATYR225

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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