› 1av8

X-ray diffraction
2.8Å resolution

Function and Biology Details

Reaction catalysed: 
2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H(2)O = ribonucleoside diphosphate + thioredoxin
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-159694 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ribonucleoside-diphosphate reductase 1 subunit beta Chains: A, B
Molecule details ›
Chains: A, B
Length: 340 amino acids
Theoretical weight: 39.6 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P69924 (Residues: 2-341; Coverage: 90%)
Gene names: JW2229, b2235, ftsB, nrdB
Sequence domains: Ribonucleotide reductase, small chain
Structure domains: Ribonucleotide Reductase, subunit A

Ligands and Environments

1 bound ligand:
Ligand FEO 2 x FEO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL7-1
Spacegroup: P61
Unit cell:
a: 139.7Å b: 139.7Å c: 110.6Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.139 0.139 0.192
Expression system: Escherichia coli

Quick links

Citations

6 review citations

Structure and function of the radical enzyme ribonucleotide reductase.
Eklund et al. (2001)
5 more

4 mentions without citation

A hot oxidant, 3-NO2Y122 radical, unmasks conformational gating in ribonucleotide reductase.
Yokoyama et al. (2010)
3 more