› 2wgh

X-ray diffraction
2.3Å resolution

Human Ribonucleotide reductase R1 subunit (RRM1) in complex with dATP and Mg.

Released:
DOI: 10.2210/pdb2wgh/pdb
PDB entry 2wgh coloured by chain, front view.
PDB entry 2wgh coloured by chain, side view.
PDB entry 2wgh coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis for allosteric regulation of human ribonucleotide reductase by nucleotide-induced oligomerization.
Fairman JW, Wijerathna SR, Ahmad MF, Xu H, Nakano R, Jha S, Prendergast J, Welin RM, Flodin S, Roos A, Nordlund P, Li Z, Walz T, Dealwis CG
Nat Struct Mol Biol 18 316-22 (2011)
PMID: 21336276

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-150119 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ribonucleoside-diphosphate reductase large subunit Chains: A, B
Molecule details ›
Chains: A, B
Length: 676 amino acids
Theoretical weight: 77.16 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P23921 (Residues: 75-742; Coverage: 84%)
Gene names: RR1, RRM1
Sequence domains:
Structure domains: Anaerobic Ribonucleotide-triphosphate Reductase Large Chain

Ligands and Environments

3 bound ligands:
Ligand GOL 1 x GOL
Ligand MG 2 x MG
Ligand DTP 2 x DTP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P21
Unit cell:
a: 66.95Å b: 129.31Å c: 76.67Å
α: 90° β: 95.5° γ: 90°
R-values:
R R work R free
0.196 0.192 0.258
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

23 review citations

Ribonucleotide reductase and cancer: biological mechanisms and targeted therapies.
Aye et al. (2015)
22 more

10 mentions without citation

The origin and evolution of ribonucleotide reduction.
Lundin et al. (2015)
9 more