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2OWQ

Crystal structure of vaccinia virus uracil-DNA glycosylase

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
B0003677molecular_functionDNA binding
B0004844molecular_functionuracil DNA N-glycosylase activity
B0006281biological_processDNA repair
B0016787molecular_functionhydrolase activity
B0016799molecular_functionhydrolase activity, hydrolyzing N-glycosyl compounds
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL A 219
ChainResidue
APRO69
ATYR70
APHE79
AASN120
AIMD401

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 B 219
ChainResidue
BHOH419
BHOH477
AILE112
AHOH433
BTHR5
BVAL6

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE IMD A 401
ChainResidue
AGLY66
AASP68
ATYR70
AASN120
ACL219

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE IMD B 402
ChainResidue
BHIS8
BALA34

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE IMD A 403
ChainResidue
AHIS8
AALA34

site_idAC6
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL B 301
ChainResidue
BGLY66
BASP68
BPRO69
BTYR70
BPRO78
BPHE79
BASN120
BHOH466
BHOH479

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL B 302
ChainResidue
BPRO10
BTHR12
BTHR14
BASP47
BPHE50

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL B 303
ChainResidue
BLYS160
BTYR180
BHIS181

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 304
ChainResidue
ALYS160
ATHR161
ATYR180
AHIS181

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 Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10072
ChainResidueDetails
AASP68
BASP68

224931

PDB entries from 2024-09-11

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