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8ILE

The crystal structure of dGTPalphaSe-Rp:DNApre-II:Pol X substrate ternary 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
B0003677molecular_functionDNA binding
B0003887molecular_functionDNA-directed DNA polymerase activity
B0006259biological_processDNA metabolic process
B0006281biological_processDNA repair
B0006284biological_processbase-excision repair
B0006303biological_processdouble-strand break repair via nonhomologous end joining
B0009059biological_processmacromolecule biosynthetic process
B0016779molecular_functionnucleotidyltransferase activity
B0044423cellular_componentvirion component
B0046872molecular_functionmetal ion binding
B0071897biological_processDNA biosynthetic process
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

220113

PDB entries from 2024-05-22

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