› 4r8u

X-ray diffraction
2.3Å resolution

Function and Biology Details

Reaction catalysed: 
Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-218977 (preferred)
Entry contents:
2 distinct polypeptide molecules
3 distinct DNA molecules
Macromolecules (5 distinct):
DNA polymerase IV Chain: A
Molecule details ›
Chain: A
Length: 340 amino acids
Theoretical weight: 38.27 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: Q47155 (Residues: 2-340; Coverage: 97%)
Gene names: JW0221, b0231, dinB, dinP
Sequence domains:
Structure domains:
DNA polymerase IV Chain: B
Molecule details ›
Chain: B
Length: 338 amino acids
Theoretical weight: 38.07 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: Q47155 (Residues: 2-338; Coverage: 96%)
Gene names: JW0221, b0231, dinB, dinP
Sequence domains:
Structure domains:
DNA Chains: C, V
Molecule details ›
Chains: C, V
Length: 17 nucleotides
Theoretical weight: 5.19 KDa
DNA Chain: W
Molecule details ›
Chain: W
Length: 18 nucleotides
Theoretical weight: 5.49 KDa
DNA Chain: D
Molecule details ›
Chain: D
Length: 16 nucleotides
Theoretical weight: 4.9 KDa

Ligands and Environments

2 bound ligands:
Ligand MG 2 x MG
Ligand 1FZ 2 x 1FZ
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06DA
Spacegroup: P21
Unit cell:
a: 86.95Å b: 57.21Å c: 110.6Å
α: 90° β: 94.69° γ: 90°
R-values:
R R work R free
0.183 0.181 0.22
Expression system: Escherichia coli

Quick links

Citations

8 review citations

Atomic-level analysis of membrane-protein structure.
Hendrickson WA. (2016)
7 more

3 mentions without citation

Native SAD is maturing.
Rose et al. (2015)
2 more