1hk8

X-ray diffraction
2.45Å resolution

STRUCTURAL BASIS FOR ALLOSTERIC SUBSTRATE SPECIFICITY REGULATION IN CLASS III RIBONUCLEOTIDE REDUCTASES: NRDD IN COMPLEX WITH DGTP

Released:

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
Macromolecule:
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
UniProt:
  • Canonical: P07071 (Residues: 1-605; Coverage: 100%)
Gene names: 49.1, 55.11/55.13, SUNY, nrdD
Structure domains: Anaerobic Ribonucleotide-triphosphate Reductase Large Chain

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX II BEAMLINE I711
Spacegroup: P43212
Unit cell:
a: 98.163Å b: 98.163Å c: 246.131Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.204 0.204 0.246
Expression system: Escherichia coli