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5HRE

The crystal structure of AsfvPolX:DNA3 binary complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0003677molecular_functionDNA binding
A0003887molecular_functionDNA-directed DNA polymerase activity
A0006259biological_processDNA metabolic process
A0006281biological_processDNA repair
A0006284biological_processbase-excision repair
A0006303biological_processdouble-strand break repair via nonhomologous end joining
A0009059biological_processmacromolecule biosynthetic process
A0016779molecular_functionnucleotidyltransferase activity
A0044423cellular_componentvirion component
A0046872molecular_functionmetal ion binding
A0071897biological_processDNA biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue MN A 201
ChainResidue
AASP49
AASP51
AFMT202
AHOH306
AHOH320
BDT9

site_idAC2
Number of Residues8
Detailsbinding site for residue FMT A 202
ChainResidue
AASP51
AMN201
AHOH306
AHOH345
BDT9
AGLY38
ASER39
AARG42

site_idAC3
Number of Residues2
Detailsbinding site for residue PO4 A 203
ChainResidue
AARG41
AHOH307

site_idAC4
Number of Residues4
Detailsbinding site for residue PO4 A 204
ChainResidue
AILE113
ATHR155
AGLU156
AHOH381

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 Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:11685239, ECO:0000305|PubMed:28245220
ChainResidueDetails
AASP49
AASP51
AASP100

site_idSWS_FT_FI2
Number of Residues1
DetailsSITE: Stabilizes dGTP in a syn confromation to overcome the Watson-Crick base pairing constraint => ECO:0000269|PubMed:24617852
ChainResidueDetails
AHIS115

219869

PDB entries from 2024-05-15

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