› 4q43

X-ray diffraction
2.45Å 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-118003 (preferred)
Entry contents:
1 distinct polypeptide molecule
2 distinct DNA molecules
Macromolecules (3 distinct):
DNA polymerase IV Chains: A, F
Molecule details ›
Chains: A, F
Length: 352 amino acids
Theoretical weight: 39.59 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: Q47155 (Residues: 2-351; Coverage: 100%)
Gene names: JW0221, b0231, dinB, dinP
Sequence domains:
Structure domains:
DNA (5'-D(*TP*CP*TP*(RDG)P*GP*GP*GP*TP*CP*CP*TP*AP*GP*GP*AP*CP*CP*C)-3') Chains: B, G
Molecule details ›
Chains: B, G
Length: 18 nucleotides
Theoretical weight: 5.59 KDa
Source organism: synthetic construct
Expression system: Not provided
DNA (5'-D(*T*CP*TP*AP*GP*GP*GP*TP*CP*CP*TP*AP*GP*GP*AP*CP*CP*C)-3') Chains: C, H
Molecule details ›
Chains: C, H
Length: 18 nucleotides
Theoretical weight: 5.49 KDa
Source organism: synthetic construct
Expression system: Not provided

Ligands and Environments

2 bound ligands:
Ligand 0KX 2 x 0KX
Ligand MG 4 x MG
1 modified residue:
Ligand RDG 2 x RDG

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06DA
Spacegroup: P21
Unit cell:
a: 85.83Å b: 56.79Å c: 112.02Å
α: 90° β: 91.96° γ: 90°
R-values:
R R work R free
0.217 0.214 0.268
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

3 review citations

How do ADARs bind RNA? New protein-RNA structures illuminate substrate recognition by the RNA editing ADARs.
Thomas et al. (2017)
2 more

4 mentions without citation

Autonomous aggregation suppression by acidic residues explains why chaperones favour basic residues.
Houben et al. (2020)
3 more