› 4i9l

X-ray diffraction
2.6Å resolution

Crystal structure of the D714A mutant of RB69 DNA polymerase

Released:
DOI: 10.2210/pdb4i9l/pdb
PDB entry 4i9l coloured by chain, front view.
PDB entry 4i9l coloured by chain, side view.
PDB entry 4i9l coloured by chain, top view.
Source organism: Escherichia phage RB69
Primary publication:
A remote palm domain residue of RB69 DNA polymerase is critical for enzyme activity and influences the conformation of the active site.
Jacewicz A, Trzemecka A, Guja KE, Plochocka D, Yakubovskaya E, Bebenek A, Garcia-Diaz M
PLoS One 8 e76700 (2013)
PMID: 24116139

Function and Biology Details

Reaction catalysed: 
Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1)
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-174312 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
DNA-directed DNA polymerase Chain: A
Molecule details ›
Chain: A
Length: 903 amino acids
Theoretical weight: 104.61 KDa
Source organism: Escherichia phage RB69
Expression system: Escherichia coli
UniProt:
  • Canonical: Q38087 (Residues: 1-903; Coverage: 100%)
Gene name: 43
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand GMP 1 x GMP
Ligand SO4 3 x SO4
Ligand CL 3 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X12C
Spacegroup: P212121
Unit cell:
a: 116.875Å b: 199.369Å c: 80.822Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.216 0.214 0.249
Expression system: Escherichia coli

Quick links

Citations

4 citation in other articles

Molecular events during translocation and proofreading extracted from 200 static structures of DNA polymerase.
Ren Z. (2016)
3 more

1 mention without citation

A remote palm domain residue of RB69 DNA polymerase is critical for enzyme activity and influences the conformation of the active site.
Jacewicz et al. (2013)