› 1osm

X-ray diffraction
3.2Å resolution

OSMOPORIN (OMPK36) FROM KLEBSIELLA PNEUMONIAE

Released:
DOI: 10.2210/pdb1osm/pdb
PDB entry 1osm coloured by chain, front view.
PDB entry 1osm coloured by chain, side view.
PDB entry 1osm coloured by chain, top view.
Source organism: Klebsiella pneumoniae
Primary publication:
Crystal structure and functional characterization of OmpK36, the osmoporin of Klebsiella pneumoniae.
Dutzler R, Rummel G, Albertí S, Hernández-Allés S, Phale P, Rosenbusch J, Benedí V, Schirmer T
Structure 7 425-34 (1999)
PMID: 10196126

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-175357 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Outer membrane porin C Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 342 amino acids
Theoretical weight: 37.63 KDa
Source organism: Klebsiella pneumoniae
Expression system: Escherichia coli
UniProt:
  • Canonical: Q48473 (Residues: 22-363; Coverage: 100%)
Gene names: ompC, ompK36
Sequence domains: Gram-negative porin
Structure domains: Porin

Ligands and Environments

1 bound ligand:
Ligand D12 9 x D12
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM1A
Spacegroup: C2
Unit cell:
a: 191.8Å b: 76.8Å c: 223.4Å
α: 90° β: 113.3° γ: 90°
R-values:
R R work R free
0.208 0.208 0.223
Expression system: Escherichia coli

Quick links

Citations

14 review citations

Molecular basis of bacterial outer membrane permeability revisited.
Nikaido H. (2003)
13 more

16 mentions without citation

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