PDBe 3r1r

X-ray diffraction
3Å resolution

RIBONUCLEOTIDE REDUCTASE R1 PROTEIN WITH AMPPNP OCCUPYING THE ACTIVITY SITE FROM ESCHERICHIA COLI

Released:

Function and Biology Details

Structure analysis Details

Assemblies composition:
hetero trimer
hetero dimer (preferred)
hetero 15-mer
hetero 12-mer
hetero nonamer
homo hexamer
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: 85.88 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:
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 K-12
Expression system: Not provided
UniProt:
  • Canonical: P69924 (Residues: 357-376; Coverage: 5%)
Gene names: JW2229, b2235, ftsB, nrdB

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X12B
Spacegroup: R32
Unit cell:
a: 224.61Å b: 224.61Å c: 336.63Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.263 not available 0.287
Expression systems:
  • Escherichia coli
  • Not provided