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5HRI

The crystal structure of AsfvPolX:DNA1 binary complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0003677molecular_functionDNA binding
A0003887molecular_functionDNA-directed DNA polymerase activity
A0006259biological_processDNA metabolic process
A0006281biological_processDNA repair
A0006303biological_processdouble-strand break repair via nonhomologous end joining
A0016779molecular_functionnucleotidyltransferase activity
A0044423cellular_componentvirion component
A0046872molecular_functionmetal ion binding
A0071897biological_processDNA biosynthetic process
B0003677molecular_functionDNA binding
B0003887molecular_functionDNA-directed DNA polymerase activity
B0006259biological_processDNA metabolic process
B0006281biological_processDNA repair
B0006303biological_processdouble-strand break repair via nonhomologous end joining
B0016779molecular_functionnucleotidyltransferase activity
B0044423cellular_componentvirion component
B0046872molecular_functionmetal ion binding
B0071897biological_processDNA biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues20
Detailsbinding site for residue DGT A 201
ChainResidue
ASER39
AVAL120
ALEU123
AARG127
AMN202
AMN203
AHOH301
AHOH303
AHOH306
AHOH309
CDC9
AARG42
DDA9
AASN48
AASP49
AASP51
AHIS115
APHE116
ATHR117
AGLY118

site_idAC2
Number of Residues5
Detailsbinding site for residue MN A 202
ChainResidue
AASP49
AASP51
ADGT201
AMN203
AHOH301

site_idAC3
Number of Residues5
Detailsbinding site for residue MN A 203
ChainResidue
AASP49
AASP51
AASP100
ADGT201
AMN202

site_idAC4
Number of Residues21
Detailsbinding site for residue DGT B 201
ChainResidue
BGLY38
BSER39
BARG42
BASN48
BASP49
BASP51
BHIS115
BPHE116
BTHR117
BGLY118
BVAL120
BLEU123
BARG127
BMN202
BMN203
BHOH302
BHOH304
BHOH307
BHOH326
FDC9
GDA9

site_idAC5
Number of Residues5
Detailsbinding site for residue MN B 202
ChainResidue
BASP49
BASP51
BDGT201
BMN203
BHOH304

site_idAC6
Number of Residues5
Detailsbinding site for residue MN B 203
ChainResidue
BASP49
BASP51
BASP100
BDGT201
BMN202

Functional Information from PROSITE/UniProt
site_idPS00522
Number of Residues20
DetailsDNA_POLYMERASE_X DNA polymerase family X signature. GSLrREekmLnDVDLLIivP
ChainResidueDetails
AGLY38-PRO57

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:11685239, ECO:0000305|PubMed:28245220
ChainResidueDetails
AASP49
AASP51
AASP100
BASP49
BASP51
BASP100

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Stabilizes dGTP in a syn confromation to overcome the Watson-Crick base pairing constraint => ECO:0000269|PubMed:24617852
ChainResidueDetails
AHIS115
BHIS115

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PDB entries from 2024-07-31

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