PDBe 3hnf

X-ray diffraction
3.16Å resolution

Crystal structure of human ribonucleotide reductase 1 bound to the effectors TTP and dATP

Released:

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
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


No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 14-ID-B
Spacegroup: P212121
Unit cell:
a: 68.856Å b: 114.388Å c: 220.003Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.189 0.185 0.26
Expression system: Escherichia coli