Function and Biology Details
Reaction catalysed:
Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1)
Biochemical function:
Biological process:
Cellular component:
- not assigned
Sequence domains:
- DNA-directed DNA polymerase, family B
- DNA polymerase family B, thumb domain
- DNA-directed DNA polymerase, family B, conserved site
- DNA polymerase alpha catalytic subunit, catalytic domain
- DNA polymerase, palm domain superfamily
- DNA/RNA polymerase superfamily
- DNA-directed DNA polymerase, family B, multifunctional domain
- Ribonuclease H superfamily
2 more domains
Structure analysis Details
Assembly composition:
hetero trimer (preferred)
Assembly name:
DNA polymerase alpha catalytic subunit and DNA (preferred)
PDBe Complex ID:
PDB-CPX-118808 (preferred)
Entry contents:
1 distinct polypeptide molecule
2 distinct DNA molecules
2 distinct DNA molecules
Macromolecules (3 distinct):
DNA polymerase alpha catalytic subunit
Molecule details ›
Chains: A, D, G, J
Length: 918 amino acids
Theoretical weight: 105.12 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains:
Length: 918 amino acids
Theoretical weight: 105.12 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
P09884 (Residues: 338-1255; Coverage: 63%)
Sequence domains:
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
NSLS BEAMLINE X25
Spacegroup:
P21
Expression systems:
- Escherichia coli
- Not provided
