2vux

X-ray diffraction
2.8Å resolution

Human ribonucleotide reductase, subunit M2 B

Released:
Source organism: Homo sapiens
Entry authors: Welin M, Moche M, Andersson J, Arrowsmith CH, Berglund H, Busam RD, Collins R, Dahlgren LG, Edwards AM, Flodin S, Flores A, Graslund S, Hammarstrom M, Herman MD, Johansson A, Johansson I, Kallas A, Karlberg T, Kotenyova T, Lehtio L, Nilsson ME, Nyman T, Persson C, Sagemark J, Schueler H, Svensson L, Thorsell AG, Tresaugues L, van Den Berg S, Weigelt J, Wikstrom M, Nordlund P, Structural Genomics Consortium (SGC)

Function and Biology Details

Reaction catalysed:
2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H(2)O = ribonucleoside diphosphate + thioredoxin
Biochemical function:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-181651 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ribonucleoside-diphosphate reductase subunit M2 B Chains: A, B
Molecule details ›
Chains: A, B
Length: 326 amino acids
Theoretical weight: 37.96 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q7LG56 (Residues: 17-322; Coverage: 87%)
Gene names: P53R2, RRM2B
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 ID23-1
Spacegroup: P212121
Unit cell:
a: 68.96Å b: 99.47Å c: 132.58Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.213 0.209 0.258
Expression system: Escherichia coli BL21(DE3)