› 2xe3

X-ray diffraction
2.85Å resolution

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-191762 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Porin OmpC Chains: A, B
Molecule details ›
Chains: A, B
Length: 343 amino acids
Theoretical weight: 38.36 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9K597 (Residues: 22-364; Coverage: 100%)
Gene names: BKL28_000773, D9D43_01315, DD762_02040, F7N46_15155, F9B07_08225, FKO60_02770, HL563_04725, ompC
Sequence domains: Gram-negative porin
Structure domains: Porin

Ligands and Environments

1 bound ligand:
Ligand BOG 2 x BOG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P63
Unit cell:
a: 103.489Å b: 103.489Å c: 186.492Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.215 0.214 0.234
Expression system: Escherichia coli

Quick links

Citations

14 review citations

Adaptive and mutational resistance: role of porins and efflux pumps in drug resistance.
Fernández et al. (2012)
13 more

5 mentions without citation

The structural biology of β-barrel membrane proteins: a summary of recent reports.
Fairman et al. (2011)
4 more