PDBe 1dml

X-ray diffraction
2.7Å resolution

CRYSTAL STRUCTURE OF HERPES SIMPLEX UL42 BOUND TO THE C-TERMINUS OF HSV POL

Released:

Function and Biology Details

Reactions catalysed:
Endonucleolytic cleavage to 5'-phosphomonoester. 
Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1). 
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
DNA polymerase catalytic subunit Chains: B, D, F, H
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:
  • Canonical: P07917 (Residues: 1200-1235; Coverage: 3%)
Gene name: UL30
Sequence domains: DNA polymerase catalytic subunit Pol
DNA polymerase processivity factor Chains: A, C, E, G
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:
  • Canonical: P10226 (Residues: 1-319; Coverage: 65%)
Gene name: UL42
Sequence domains: DNA polymerase processivity factor (UL42)
Structure domains: Proliferating Cell Nuclear Antigen

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SIEMENS
Spacegroup: P21
Unit cell:
a: 54.32Å b: 100.07Å c: 129.53Å
α: 90° β: 100.62° γ: 90°
R-values:
R R work R free
0.23 0.23 0.281
Expression system: Escherichia coli