› 5r1r

X-ray diffraction
3.1Å resolution

RIBONUCLEOTIDE REDUCTASE E441A MUTANT R1 PROTEIN FROM ESCHERICHIA COLI

Released:
DOI: 10.2210/pdb5r1r/pdb
PDB entry 5r1r coloured by chain, front view.
PDB entry 5r1r coloured by chain, side view.
PDB entry 5r1r coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
A new mechanism-based radical intermediate in a mutant R1 protein affecting the catalytically essential Glu441 in Escherichia coli ribonucleotide reductase.
Persson AL, Eriksson M, Katterle B, Pötsch S, Sahlin M, Sjöberg BM
J Biol Chem 272 31533-41 (1997)
PMID: 9395490

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

Assemblies composition:
hetero trimer
hetero tetramer
hetero dimer (preferred)
hetero dodecamer
hetero hexamer
homo hexamer
Assembly name:
PDBe Complex ID:
PDB-CPX-132526 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Ribonucleoside-diphosphate reductase 1 subunit alpha Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 761 amino acids
Theoretical weight: 85.82 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
Ribonucleoside-diphosphate reductase 1 subunit beta Chains: D, E, F, P
Molecule details ›
Chains: D, E, F, P
Length: 20 amino acids
Theoretical weight: 2.27 KDa
Source organism: Escherichia coli
Expression system: Not provided
UniProt:
  • Canonical: P69924 (Residues: 357-376; Coverage: 5%)
Gene names: JW2229, b2235, ftsB, nrdB

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS
Spacegroup: R32
Unit cell:
a: 223.81Å b: 223.81Å c: 334.26Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.199 0.196 0.227
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

8 review citations

Structure and function of the radical enzyme ribonucleotide reductase.
Eklund et al. (2001)
7 more

1 mention without citation

Isolation and characterization of a cyanophage infecting the toxic cyanobacterium Microcystis aeruginosa.
Yoshida et al. (2006)