3vpm

X-ray diffraction
2.7Å resolution

Crystal structure of human ribonucleotide reductase subunit M2 (hRRM2) mutant

Released:
Source organism: Homo sapiens
Entry authors: Chen X, Xu Z, Liu H, Zhang L, Chen B, Zhu L, Yang C, Zhu W, Shao J

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)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ribonucleoside-diphosphate reductase subunit M2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 286 amino acids
Theoretical weight: 33.56 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P31350 (Residues: 66-350; Coverage: 73%)
Gene names: RR2, RRM2
Sequence domains: Ribonucleotide reductase, small chain
Structure domains: Ribonucleotide Reductase, subunit A

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: P43212
Unit cell:
a: 108.998Å b: 108.998Å c: 174.948Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.209 0.207 0.249
Expression system: Escherichia coli