Function and Biology Details
Reaction catalysed:
Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1)
Biochemical function:
Biological process:
Cellular component:
- not assigned
Structure analysis Details
Assembly composition:
hetero trimer (preferred)
PDBe Complex ID:
PDB-CPX-146555 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
DNA polymerase alpha subunit B
Molecule details ›
Chains: A, C, E, G
Length: 460 amino acids
Theoretical weight: 51.96 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
Sequence domains: DNA polymerase alpha/epsilon subunit B
Structure domains: Purple Acid Phosphatase; chain A, domain 2
Length: 460 amino acids
Theoretical weight: 51.96 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
- Canonical:
P38121 (Residues: 246-705; Coverage: 65%)
Sequence domains: DNA polymerase alpha/epsilon subunit B
Structure domains: Purple Acid Phosphatase; chain A, domain 2
DNA polymerase alpha catalytic subunit A
Molecule details ›
Chains: B, D, F, H
Length: 206 amino acids
Theoretical weight: 23.98 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
Sequence domains: DNA Polymerase alpha zinc finger
Structure domains: DNA Polymerase alpha, zinc finger
Length: 206 amino acids
Theoretical weight: 23.98 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
- Canonical: P13382 (Residues: 1263-1468; Coverage: 14%)
Sequence domains: DNA Polymerase alpha zinc finger
Structure domains: DNA Polymerase alpha, zinc finger
