› 1mrr

X-ray diffraction
2.5Å resolution

SUBSTITUTION OF MANGANESE FOR IRON IN RIBONUCLEOTIDE REDUCTASE FROM ESCHERICHIA COLI. SPECTROSCOPIC AND CRYSTALLOGRAPHIC CHARACTERIZATION

Released:
DOI: 10.2210/pdb1mrr/pdb
PDB entry 1mrr coloured by chain, front view.
PDB entry 1mrr coloured by chain, side view.
PDB entry 1mrr coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Substitution of manganese for iron in ribonucleotide reductase from Escherichia coli. Spectroscopic and crystallographic characterization.
Atta M, Nordlund P, Aberg A, Eklund H, Fontecave M
J Biol Chem 267 20682-8 (1992)
PMID: 1328209

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: 43.37 KDa
Source organism: Escherichia coli
Expression system: Not provided
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 MN 4 x MN
Ligand HG 13 x HG
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 74.3Å b: 85.5Å c: 115.7Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.18 0.18 not available
Expression system: Not provided

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Citations

11 review citations

The ferritins: molecular properties, iron storage function and cellular regulation.
Harrison et al. (1996)
10 more

2 mentions without citation

Prediction of ligand binding sites using homologous structures and conservation at CASP8.
Wass et al. (2009)
1 more