Function and Biology Details
Reactions catalysed:
Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1)
Endonucleolytic cleavage to 5'-phosphomonoester.
Biochemical function:
Biological process:
Cellular component:
- not assigned
Sequence domains:
Structure domain:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139840 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
DNA polymerase processivity factor
Molecule details ›
Chains: A, C, E, G
Length: 319 amino acids
Theoretical weight: 34.23 KDa
Source organism: Human alphaherpesvirus 1
Expression system: Escherichia coli
UniProt:
Sequence domains: DNA polymerase processivity factor (UL42)
Structure domains: Proliferating Cell Nuclear Antigen
Length: 319 amino acids
Theoretical weight: 34.23 KDa
Source organism: Human alphaherpesvirus 1
Expression system: Escherichia coli
UniProt:
- Canonical:
P10226 (Residues: 1-319; Coverage: 65%)
Sequence domains: DNA polymerase processivity factor (UL42)
Structure domains: Proliferating Cell Nuclear Antigen
DNA polymerase catalytic subunit
Molecule details ›
Chains: B, D, F, H
Length: 36 amino acids
Theoretical weight: 3.75 KDa
Source organism: Human alphaherpesvirus 1
Expression system: Escherichia coli
UniProt:
Sequence domains: DNA polymerase catalytic subunit Pol
Length: 36 amino acids
Theoretical weight: 3.75 KDa
Source organism: Human alphaherpesvirus 1
Expression system: Escherichia coli
UniProt:
- Canonical: P07917 (Residues: 1200-1235; Coverage: 3%)
Sequence domains: DNA polymerase catalytic subunit Pol
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
SIEMENS
Spacegroup:
P21
Expression system: Escherichia coli
