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2BOO

The crystal structure of Uracil-DNA N-Glycosylase (UNG) from Deinococcus radiodurans.

Functional Information from GO Data
ChainGOidnamespacecontents
A0004844molecular_functionuracil DNA N-glycosylase activity
A0005737cellular_componentcytoplasm
A0006281biological_processDNA repair
A0006284biological_processbase-excision repair
A0006974biological_processDNA damage response
A0016787molecular_functionhydrolase activity
A0016799molecular_functionhydrolase activity, hydrolyzing N-glycosyl compounds
A0097510biological_processbase-excision repair, AP site formation via deaminated base removal
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NO3 A1247
ChainResidue
AGLN82
AASP83
ASER95
APHE96
AASN142
AHOH2154

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE NO3 A1248
ChainResidue
ASER204
AGLY205
ALEU210
ASER211
AGLN213
ATYR214
AGLY184
ASER185
AARG188

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE NO3 A1249
ChainResidue
ALEU47
AARG51
AVAL63

Functional Information from PROSITE/UniProt
site_idPS00130
Number of Residues10
DetailsU_DNA_GLYCOSYLASE Uracil-DNA glycosylase signature. KVLIlGQDPY
ChainResidueDetails
ALYS76-TYR85

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00148","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1eug
ChainResidueDetails
AASP83
AHIS206

239149

PDB entries from 2025-07-23

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