› 2r1r

X-ray diffraction
3Å resolution

RIBONUCLEOTIDE REDUCTASE R1 PROTEIN WITH DTTP OCCUPYING THE SPECIFICITY SITE FROM ESCHERICHIA COLI

Released:
DOI: 10.2210/pdb2r1r/pdb
PDB entry 2r1r coloured by chain, front view.
PDB entry 2r1r coloured by chain, side view.
PDB entry 2r1r coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Binding of allosteric effectors to ribonucleotide reductase protein R1: reduction of active-site cysteines promotes substrate binding.
Eriksson M, Uhlin U, Ramaswamy S, Ekberg M, Regnström K, Sjöberg BM, Eklund H
Structure 5 1077-92 (1997)
PMID: 9309223

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 dimer (preferred)
hetero dodecamer
hetero tetramer
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: 85.88 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:
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

1 bound ligand:
Ligand TTP 3 x TTP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX9.6
Spacegroup: R32
Unit cell:
a: 227.82Å b: 227.82Å c: 343.47Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.26 0.238 0.28
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

26 review citations

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

7 mentions without citation

From Deep Mutational Mapping of Allosteric Protein Landscapes to Deep Learning of Allostery and Hidden Allosteric Sites: Zooming in on "Allosteric Intersection" of Biochemical and Big Data Approaches.
Verkhivker et al. (2023)
6 more