› 3hnd

X-ray diffraction
3.21Å resolution

Crystal structure of human ribonucleotide reductase 1 bound to the effector TTP and substrate GDP

Released:
DOI: 10.2210/pdb3hnd/pdb
PDB entry 3hnd coloured by chain, front view.
PDB entry 3hnd coloured by chain, side view.
PDB entry 3hnd 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:
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: 792 amino acids
Theoretical weight: 90.18 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P23921 (Residues: 1-792; Coverage: 100%)
Gene names: RR1, RRM1
Sequence domains:
Structure domains: Anaerobic Ribonucleotide-triphosphate Reductase Large Chain

Ligands and Environments

4 bound ligands:
Ligand MG 2 x MG
Ligand TTP 2 x TTP
Ligand GDP 2 x GDP
Ligand SO4 4 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-B
Spacegroup: P212121
Unit cell:
a: 73.159Å b: 115.834Å c: 221.305Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.183 0.18 0.254
Expression system: Escherichia coli

Quick links

Citations

24 review citations

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

10 mentions without citation

The more the merrier: how homo-oligomerization alters the interactome and function of ribonucleotide reductase.
Long et al. (2020)
9 more