5HR9

The crystal structure of Se-AsfvPolX(L52/163M mutant) in complex with 1nt-gap DNA1

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003677	molecular_function	DNA binding
A	0003887	molecular_function	DNA-directed DNA polymerase activity
A	0006259	biological_process	DNA metabolic process
A	0006281	biological_process	DNA repair
A	0006303	biological_process	double-strand break repair via nonhomologous end joining
A	0016779	molecular_function	nucleotidyltransferase activity
A	0034061	molecular_function	DNA polymerase activity
A	0044423	cellular_component	virion component
A	0046872	molecular_function	metal ion binding
A	0071897	biological_process	DNA biosynthetic process
B	0003677	molecular_function	DNA binding
B	0003887	molecular_function	DNA-directed DNA polymerase activity
B	0006259	biological_process	DNA metabolic process
B	0006281	biological_process	DNA repair
B	0006303	biological_process	double-strand break repair via nonhomologous end joining
B	0016779	molecular_function	nucleotidyltransferase activity
B	0034061	molecular_function	DNA polymerase activity
B	0044423	cellular_component	virion component
B	0046872	molecular_function	metal ion binding
B	0071897	biological_process	DNA biosynthetic process

Functional Information from PROSITE/UniProt

site_id	PS00522
Number of Residues	20
Details	DNA_POLYMERASE_X DNA polymerase family X signature. GSLrREekmLnDVDMLIivP

Chain	Residue	Details
A	GLY38-PRO57

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269|PubMed:11685239, ECO:0000305|PubMed:28245220

Chain	Residue	Details
A	ASP49
A	ASP51
A	ASP100
B	ASP49
B	ASP51
B	ASP100

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site_id	SWS_FT_FI2
Number of Residues	2
Details	SITE: Stabilizes dGTP in a syn confromation to overcome the Watson-Crick base pairing constraint => ECO:0000269|PubMed:24617852

Chain	Residue	Details
A	HIS115
B	HIS115

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