› 1xsm

X-ray diffraction
2.3Å resolution

PROTEIN R2 OF RIBONUCLEOTIDE REDUCTASE FROM MOUSE

Released:
DOI: 10.2210/pdb1xsm/pdb
PDB entry 1xsm coloured by chain, front view.
PDB entry 1xsm coloured by chain, side view.
PDB entry 1xsm coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
The three-dimensional structure of mammalian ribonucleotide reductase protein R2 reveals a more-accessible iron-radical site than Escherichia coli R2.
Kauppi B, Nielsen BB, Ramaswamy S, Larsen IK, Thelander M, Thelander L, Eklund H
J Mol Biol 262 706-20 (1996)
PMID: 8876648

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 FE 1 x FE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX9.6
Spacegroup: C2221
Unit cell:
a: 77.078Å b: 108.932Å c: 92.9Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.191 0.191 0.25
Expression system: Escherichia coli

Quick links

Citations

10 review citations

Ribonucleotide reductases.
Jordan et al. (1998)
9 more

6 mentions without citation

A new method of identifying the site of tyrosyl radicals in proteins.
Svistunenko et al. (2004)
5 more