› 1rlr

X-ray diffraction
2.5Å resolution

STRUCTURE OF RIBONUCLEOTIDE REDUCTASE PROTEIN R1

Released:
DOI: 10.2210/pdb1rlr/pdb
PDB entry 1rlr coloured by chain, front view.
PDB entry 1rlr coloured by chain, side view.
PDB entry 1rlr coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structure of ribonucleotide reductase protein R1.
Uhlin U, Eklund H
Nature 370 533-9 (1994)
PMID: 8052308

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 domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132524 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ribonucleoside-diphosphate reductase 1 subunit alpha Chain: A
Molecule details ›
Chain: A
Length: 761 amino acids
Theoretical weight: 86.01 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P00452 (Residues: 1-761; Coverage: 100%)
Gene names: JW2228, b2234, dnaF, nrdA
Sequence domains:
Structure domains: Anaerobic Ribonucleotide-triphosphate Reductase Large Chain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: R32
Unit cell:
a: 226Å b: 226Å c: 341Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.21 0.21 not available
Expression system: Escherichia coli

Quick links

Citations

48 review citations

Ribonucleotide reductases.
Nordlund et al. (2006)
47 more

11 mentions without citation

Thioredoxin and glutaredoxin-mediated redox regulation of ribonucleotide reductase.
Sengupta et al. (2014)
10 more