› 5ci2

X-ray diffraction
2.25Å 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 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 Chain: A
Molecule details ›
Chain: A
Length: 375 amino acids
Theoretical weight: 43.48 KDa
Source organism: Escherichia coli O157:H7
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P69924 (Residues: 2-376; Coverage: 100%)
Gene names: JW2229, b2235, ftsB, nrdB
Sequence domains: Ribonucleotide reductase, small chain
Structure domains: Ribonucleotide Reductase, subunit A

Ligands and Environments

2 bound ligands:
Ligand FEO 1 x FEO
Ligand SO4 4 x SO4
1 modified residue:
Ligand 51T 1 x 51T

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: P6122
Unit cell:
a: 91.42Å b: 91.42Å c: 206.607Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.173 0.172 0.197
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

Playing with the Molecules of Life.
Young et al. (2018)
1 more

1 mention without citation

Biophysical Characterization of Fluorotyrosine Probes Site-Specifically Incorporated into Enzymes: E. coli Ribonucleotide Reductase As an Example.
Oyala et al. (2016)