› 1hxt

X-ray diffraction
2.4Å resolution

OMPF PORIN MUTANT NQAAA

Released:
DOI: 10.2210/pdb1hxt/pdb
PDB entry 1hxt coloured by chain, front view.
PDB entry 1hxt coloured by chain, side view.
PDB entry 1hxt coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Role of charged residues at the OmpF porin channel constriction probed by mutagenesis and simulation.
Phale PS, Philippsen A, Widmer C, Phale VP, Rosenbusch JP, Schirmer T
Biochemistry 40 6319-25 (2001)
PMID: 11371193

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-136399 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Outer membrane porin F Chain: A
Molecule details ›
Chain: A
Length: 340 amino acids
Theoretical weight: 36.85 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P02931 (Residues: 23-362; Coverage: 100%)
Gene names: JW0912, b0929, cmlB, coa, cry, ompF, tolF
Sequence domains: Gram-negative porin
Structure domains: Porin

Ligands and Environments

1 bound ligand:
Ligand C8E 10 x C8E
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X11
Spacegroup: P321
Unit cell:
a: 117.084Å b: 117.084Å c: 51.344Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.233 0.233 0.289
Expression system: Escherichia coli

Quick links

Citations

16 review citations

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

5 mentions without citation

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