› 1h0o

X-ray diffraction
2.2Å resolution

Cobalt substitution of mouse R2 ribonucleotide reductase to model the reactive diferrous state

Released:
DOI: 10.2210/pdb1h0o/pdb
PDB entry 1h0o coloured by chain, front view.
PDB entry 1h0o coloured by chain, side view.
PDB entry 1h0o coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Cobalt substitution of mouse R2 ribonucleotide reductase as a model for the reactive diferrous state: spectroscopic and structural evidence for a ferromagnetically coupled dinuclear cobalt cluster.
Strand KR, Karlsen S, Andersson KK
J Biol Chem 277 34229-38 (2002)
PMID: 12087093

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-145687 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ribonucleoside-diphosphate reductase subunit M2 Chain: A
Molecule details ›
Chain: A
Length: 390 amino acids
Theoretical weight: 45.15 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: P11157 (Residues: 1-390; Coverage: 100%)
Gene name: Rrm2
Sequence domains: Ribonucleotide reductase, small chain
Structure domains: Ribonucleotide Reductase, subunit A

Ligands and Environments

1 bound ligand:
Ligand CO 1 x CO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: C2221
Unit cell:
a: 75.9Å b: 106.57Å c: 91.62Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.235 0.235 0.282
Expression system: Escherichia coli

Quick links

Citations

4 citation in other articles

The binding of iron and zinc to glyoxalase II occurs exclusively as di-metal centers and is unique within the metallo-beta-lactamase family.
Wenzel et al. (2004)
3 more