X-ray diffraction
2.8Å resolution

Crystal structure of human ribonucleotide reductase subunit R2

Source organism: Homo sapiens
Entry authors: Welin M, Ogg D, Arrowsmith C, Berglund H, Busam R, Collins R, Edwards A, Ehn M, Flodin S, Flores A, Graslund S, Hammarstrom M, Hallberg BM, Holmberg Schiavone L, Hogbom M, Kotenyova T, Magnusdottir A, Moche M, Nilsson-Ehle P, Nyman T, Persson C, Sagemark J, Sundstrom M, Stenmark P, Uppenberg J, Thorsell AG, Van Den Berg S, Wallden K, Weigelt J, Nordlund P

Function and Biology Details

Reaction catalysed:
2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H(2)O = ribonucleoside diphosphate + thioredoxin
Biochemical function:
Biological process:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Ribonucleoside-diphosphate reductase subunit M2 Chain: A
Molecule details ›
Chain: A
Length: 332 amino acids
Theoretical weight: 38.69 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
  • Canonical: P31350 (Residues: 60-389; Coverage: 85%)
Gene names: RR2, RRM2
Sequence domains: Ribonucleotide reductase, small chain
Structure domains: Ribonucleotide Reductase, subunit A

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: C2221
Unit cell:
a: 76.12Å b: 110.7Å c: 94.42Å
α: 90° β: 90° γ: 90°
R R work R free
0.233 0.23 0.294
Expression system: Escherichia coli BL21(DE3)