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3NT7

Crystal Structure of Vaccinia Virus Uracil DNA Glycosylase R187V Mutant

Functional Information from GO Data
ChainGOidnamespacecontents
A0003677molecular_functionDNA binding
A0004844molecular_functionuracil DNA N-glycosylase activity
A0006281biological_processDNA repair
A0016787molecular_functionhydrolase activity
A0016799molecular_functionhydrolase activity, hydrolyzing N-glycosyl compounds
C0003677molecular_functionDNA binding
C0004844molecular_functionuracil DNA N-glycosylase activity
C0006281biological_processDNA repair
C0016787molecular_functionhydrolase activity
C0016799molecular_functionhydrolase activity, hydrolyzing N-glycosyl compounds
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 C 219
ChainResidue
CGLY159
CLYS160
CTHR161
CTYR180
CHIS181

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 C 220
ChainResidue
AARG98
AHOH238
CARG98

site_idAC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE GOL C 221
ChainResidue
CASN199

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 219
ChainResidue
AGLY159
ALYS160
ATYR180
AHIS181

Functional Information from PROSITE/UniProt
site_idPS00130
Number of Residues10
DetailsU_DNA_GLYCOSYLASE Uracil-DNA glycosylase signature. RVCVcGIDPY
ChainResidueDetails
CARG61-TYR70

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10072
ChainResidueDetails
CASP68
AASP68

223790

PDB entries from 2024-08-14

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