› 1piz

X-ray diffraction
1.9Å resolution

RIBONUCLEOTIDE REDUCTASE R2 D84E MUTANT SOAKED WITH FERROUS IONS AT NEUTRAL PH

Released:
DOI: 10.2210/pdb1piz/pdb
PDB entry 1piz coloured by chain, front view.
PDB entry 1piz coloured by chain, side view.
PDB entry 1piz coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Variable coordination geometries at the diiron(II) active site of ribonucleotide reductase R2.
Voegtli WC, Sommerhalter M, Saleh L, Baldwin J, Bollinger JM, Rosenzweig AC
J Am Chem Soc 125 15822-30 (2003)
PMID: 14677973

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: 375 amino acids
Theoretical weight: 43.43 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
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 FE 4 x FE
Ligand HG 11 x HG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-1
Spacegroup: P212121
Unit cell:
a: 74Å b: 84.2Å c: 114.2Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.21 0.207 0.242
Expression system: Escherichia coli

Quick links

Citations

7 review citations

Class I ribonucleotide reductases: metallocofactor assembly and repair in vitro and in vivo.
Cotruvo et al. (2011)
6 more

1 mention without citation

Spectroscopic studies of single and double variants of M ferritin: lack of conversion of a biferrous substrate site into a cofactor site for O2 activation.
Kwak et al. (2014)