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4ODA

Crystal structure of the vaccinia virus DNA polymerase holoenzyme subunit D4 in complex with the A20 N-terminus

Functional Information from GO Data
ChainGOidnamespacecontents
A0003677molecular_functionDNA binding
A0004844molecular_functionuracil DNA N-glycosylase activity
A0005515molecular_functionprotein binding
A0006281biological_processDNA repair
A0016787molecular_functionhydrolase activity
A0016799molecular_functionhydrolase activity, hydrolyzing N-glycosyl compounds
A0039693biological_processviral DNA genome replication
B0003677molecular_functionDNA binding
B0004844molecular_functionuracil DNA N-glycosylase activity
B0005515molecular_functionprotein binding
B0006281biological_processDNA repair
B0016787molecular_functionhydrolase activity
B0016799molecular_functionhydrolase activity, hydrolyzing N-glycosyl compounds
B0039693biological_processviral DNA genome replication
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 301
ChainResidue
BLYS86
BLYS87
BHOH449

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 B 302
ChainResidue
BHOH431
BTYR70
BPRO71
BSER88
BHIS181
BGOL304
BHOH417

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 B 303
ChainResidue
BGLY159
BLYS160
BTHR161
BTYR180
BHIS181
BALA184
BHOH401

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL B 304
ChainResidue
BGLY66
BASP68
BPRO78
BPHE79
BASN120
BSO4302
BHOH402

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 301
ChainResidue
ATHR85
ALYS86
ALYS87
AHOH413

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 302
ChainResidue
AGLY159
ALYS160
ATHR161
ATYR180
AHIS181
AALA184
AHOH429

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 303
ChainResidue
ATYR70
APRO71
ASER88
AHIS181
AGOL304
AHOH413
AHOH414

site_idAC8
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 304
ChainResidue
AGLY66
AASP68
APRO69
ATYR70
APRO78
APHE79
AASN120
ASO4303
AHOH401

Functional Information from PROSITE/UniProt
site_idPS00130
Number of Residues10
DetailsU_DNA_GLYCOSYLASE Uracil-DNA glycosylase signature. RVCVcGIDPY
ChainResidueDetails
BARG61-TYR70

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10072
ChainResidueDetails
BASP68
AASP68

219869

PDB entries from 2024-05-15

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