1xje

X-ray diffraction
1.9Å resolution

Structural mechanism of allosteric substrate specificity in a ribonucleotide reductase: dTTP-GDP complex

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Vitamin B12-dependent ribonucleotide reductase Chains: A, B
Molecule details ›
Chains: A, B
Length: 644 amino acids
Theoretical weight: 73.37 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O33839 (Residues: 1-644; Coverage: 78%)
Gene name: nrdJ
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: EMBL/DESY, HAMBURG BEAMLINE X11
Spacegroup: C2
Unit cell:
a: 119.391Å b: 124.376Å c: 107.243Å
α: 90° β: 103.68° γ: 90°
R-values:
R R work R free
0.184 0.182 0.223
Expression system: Escherichia coli BL21(DE3)