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2J8X

Epstein-Barr virus uracil-DNA glycosylase in complex with Ugi from PBS-2

Functional Information from GO Data
ChainGOidnamespacecontents
A0004844molecular_functionuracil DNA N-glycosylase activity
A0006281biological_processDNA repair
A0006284biological_processbase-excision repair
A0016787molecular_functionhydrolase activity
A0016799molecular_functionhydrolase activity, hydrolyzing N-glycosyl compounds
A0042025cellular_componenthost cell nucleus
A0097510biological_processbase-excision repair, AP site formation via deaminated base removal
B0005515molecular_functionprotein binding
C0004844molecular_functionuracil DNA N-glycosylase activity
C0006281biological_processDNA repair
C0006284biological_processbase-excision repair
C0016787molecular_functionhydrolase activity
C0016799molecular_functionhydrolase activity, hydrolyzing N-glycosyl compounds
C0042025cellular_componenthost cell nucleus
C0097510biological_processbase-excision repair, AP site formation via deaminated base removal
D0005515molecular_functionprotein binding
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE URE B1085
ChainResidue
AGLY160
AALA163
BASP61

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE URE D1085
ChainResidue
CGLY160
CALA163
DASP61

Functional Information from PROSITE/UniProt
site_idPS00130
Number of Residues10
DetailsU_DNA_GLYCOSYLASE Uracil-DNA glycosylase signature. KVVIlGQDPY
ChainResidueDetails
ALYS84-TYR93

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_04046
ChainResidueDetails
AASP91
CASP91

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1eug
ChainResidueDetails
AASP91
AHIS213

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1eug
ChainResidueDetails
CASP91
CHIS213

222415

PDB entries from 2024-07-10

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