› 1rnr

X-ray diffraction
2.5Å resolution

AUTOCATALYTIC GENERATION OF DOPA IN THE ENGINEERED PROTEIN R2 F208Y FROM ESCHERICHIA COLI RIBONUCLEOTIDE REDUCTASE AND CRYSTAL STRUCTURE OF THE DOPA-208 PROTEIN

Released:
DOI: 10.2210/pdb1rnr/pdb
PDB entry 1rnr coloured by chain, front view.
PDB entry 1rnr coloured by chain, side view.
PDB entry 1rnr coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Autocatalytic generation of dopa in the engineered protein R2 F208Y from Escherichia coli ribonucleotide reductase and crystal structure of the dopa-208 protein.
Aberg A, Ormö M, Nordlund P, Sjöberg BM
Biochemistry 32 9845-50 (1993)
PMID: 8373782

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 domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-159694 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ribonucleoside-diphosphate reductase 1 subunit beta Chains: A, B
Molecule details ›
Chains: A, B
Length: 375 amino acids
Theoretical weight: 43.4 KDa
Source organism: Escherichia coli
Expression system: Not provided
UniProt:
  • Canonical: P69924 (Residues: 2-376; Coverage: 100%)
Gene names: JW2229, b2235, ftsB, nrdB
Sequence domains: Ribonucleotide reductase, small chain
Structure domains: Ribonucleotide Reductase, subunit A

Ligands and Environments

2 bound ligands:
Ligand FE 4 x FE
Ligand HG 14 x HG
1 modified residue:
Ligand DAH 2 x DAH

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 74.1Å b: 85.3Å c: 115.7Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.186 0.186 not available
Expression system: Not provided

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Citations

4 review citations

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