PDBe 3hnc

X-ray diffraction
2.41Å resolution

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

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

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-B
Spacegroup: P212121
Unit cell:
a: 68.98Å b: 114.104Å c: 219.283Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.188 0.186 0.236
Expression system: Escherichia coli