› 2wvp

X-ray diffraction
2.4Å resolution

Synthetically modified OmpG

Released:
DOI: 10.2210/pdb2wvp/pdb
PDB entry 2wvp coloured by chain, front view.
PDB entry 2wvp coloured by chain, side view.
PDB entry 2wvp coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Structural and functional characterization of a synthetically modified OmpG.
Grosse W, Reiss P, Reitz S, Cebi M, Lübben W, Koert U, Essen LO
Bioorg Med Chem 18 7716-23 (2010)
PMID: 20378361

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-160039 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Outer membrane porin G Chain: A
Molecule details ›
Chain: A
Length: 286 amino acids
Theoretical weight: 33.57 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P76045 (Residues: 22-301; Coverage: 100%)
Gene names: JW1312, b1319, ompG
Sequence domains: Outer membrane protein G (OmpG)
Structure domains: monomeric porin ompg

Ligands and Environments

3 bound ligands:
Ligand 420 1 x 420
Ligand C8E 6 x C8E
Ligand EDO 1 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: C2
Unit cell:
a: 99.56Å b: 69.81Å c: 59.13Å
α: 90° β: 103.6° γ: 90°
R-values:
R R work R free
0.224 0.221 0.287
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

Strategies and perspectives in ion-channel engineering.
Grosse et al. (2011)
1 more

2 mentions without citation

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