X-ray diffraction
2.45Å resolution

Structural basis for allosteric substrate specificity regulation in class III ribonucleotide reductases, native NRDD


Function and Biology Details

Reaction catalysed:
Ribonucleoside 5'-triphosphate + formate = 2'-deoxyribonucleoside 5'-triphosphate + CO(2) + H(2)O
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Anaerobic ribonucleoside-triphosphate reductase Chain: A
Molecule details ›
Chain: A
Length: 605 amino acids
Theoretical weight: 68.06 KDa
Source organism: Escherichia virus T4
Expression system: Escherichia coli
  • Canonical: P07071 (Residues: 1-605; Coverage: 100%)
Gene names: 49.1, 55.11/55.13, SUNY, nrdD
Sequence domains: Glycine radical
Structure domains: Anaerobic Ribonucleotide-triphosphate Reductase Large Chain

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX II BEAMLINE I711
Spacegroup: P43212
Unit cell:
a: 98.019Å b: 98.019Å c: 242.421Å
α: 90° β: 90° γ: 90°
R R work R free
0.224 0.224 0.258
Expression system: Escherichia coli