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4DOF

Structures of Vaccinia Virus Uracil-DNA Glycosylase in New Crystal Forms

Functional Information from GO Data
ChainGOidnamespacecontents
A0003677molecular_functionDNA binding
A0004844molecular_functionuracil DNA N-glycosylase activity
A0006281biological_processDNA repair
A0006974biological_processDNA damage response
A0016787molecular_functionhydrolase activity
A0016799molecular_functionhydrolase activity, hydrolyzing N-glycosyl compounds
B0003677molecular_functionDNA binding
B0004844molecular_functionuracil DNA N-glycosylase activity
B0006281biological_processDNA repair
B0006974biological_processDNA damage response
B0016787molecular_functionhydrolase activity
B0016799molecular_functionhydrolase activity, hydrolyzing N-glycosyl compounds
C0003677molecular_functionDNA binding
C0004844molecular_functionuracil DNA N-glycosylase activity
C0006281biological_processDNA repair
C0006974biological_processDNA damage response
C0016787molecular_functionhydrolase activity
C0016799molecular_functionhydrolase activity, hydrolyzing N-glycosyl compounds
D0003677molecular_functionDNA binding
D0004844molecular_functionuracil DNA N-glycosylase activity
D0006281biological_processDNA repair
D0006974biological_processDNA damage response
D0016787molecular_functionhydrolase activity
D0016799molecular_functionhydrolase activity, hydrolyzing N-glycosyl compounds
Functional Information from PROSITE/UniProt
site_idPS00130
Number of Residues10
DetailsU_DNA_GLYCOSYLASE Uracil-DNA glycosylase signature. RVCVcGIDPY
ChainResidueDetails
AARG61-TYR70

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10072","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

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PDB entries from 2025-10-29

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