› 1h7b

X-ray diffraction
2.45Å resolution

Structural basis for allosteric substrate specificity regulation in class III ribonucleotide reductases, native NRDD

Released:
DOI: 10.2210/pdb1h7b/pdb
PDB entry 1h7b coloured by chain, front view.
PDB entry 1h7b coloured by chain, side view.
PDB entry 1h7b coloured by chain, top view.
Source organism: Escherichia virus T4
Primary publication:
Structural basis for allosteric substrate specificity regulation in anaerobic ribonucleotide reductases.
Larsson KM, Andersson J, Sjöberg BM, Nordlund P, Logan DT
Structure 9 739-50 (2001)
PMID: 11587648

Function and Biology Details

Reaction catalysed: 
Ribonucleoside 5'-triphosphate + formate = 2'-deoxyribonucleoside 5'-triphosphate + CO(2) + H(2)O
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139363 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Anaerobic ribonucleoside-triphosphate reductase Chain: A
Molecule details ›
Chain: A
Length: 605 amino acids
Theoretical weight: 68.06 KDa
Source organism: Escherichia virus T4
Expression system: Escherichia coli
UniProt:
  • Canonical: P07071 (Residues: 1-605; Coverage: 100%)
Gene names: 49.1, 55.11/55.13, SUNY, nrdD
Sequence domains: Glycine radical
Structure domains: Anaerobic Ribonucleotide-triphosphate Reductase Large Chain

Ligands and Environments

1 bound ligand:
Ligand PO4 1 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX II BEAMLINE I711
Spacegroup: P43212
Unit cell:
a: 98.019Å b: 98.019Å c: 242.421Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.224 0.224 0.258
Expression system: Escherichia coli

Quick links

Citations

7 review citations

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

3 mentions without citation

The origin and evolution of ribonucleotide reduction.
Lundin et al. (2015)
2 more