› 1nye

X-ray diffraction
2.4Å resolution

Crystal structure of OsmC from E. coli

Released:
DOI: 10.2210/pdb1nye/pdb
PDB entry 1nye coloured by chain, front view.
PDB entry 1nye coloured by chain, side view.
PDB entry 1nye coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structure of OsmC from Escherichia coli: a salt-shock-induced protein.
Shin DH, Choi IG, Busso D, Jancarik J, Yokota H, Kim R, Kim SH
Acta Crystallogr D Biol Crystallogr 60 903-11 (2004)
PMID: 15103136

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
homo hexamer
Assembly name:
PDBe Complex ID:
PDB-CPX-142892 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peroxiredoxin OsmC Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 162 amino acids
Theoretical weight: 17.45 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0C0L2 (Residues: 1-143; Coverage: 100%)
Gene names: JW1477, b1482, osmC
Sequence domains: OsmC-like protein
Structure domains: GMP Synthetase; Chain A, domain 3

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.2
Spacegroup: P21
Unit cell:
a: 49.529Å b: 90.291Å c: 112.677Å
α: 90° β: 93.9° γ: 90°
R-values:
R R work R free
0.224 0.218 0.277
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Conservation and diversity of radiation and oxidative stress resistance mechanisms in Deinococcus species.
Lim et al. (2019)
1 more

2 mentions without citation

Non-homologous isofunctional enzymes: a systematic analysis of alternative solutions in enzyme evolution.
Omelchenko et al. (2010)
1 more