› 1prn

X-ray diffraction
1.96Å resolution

REFINED STRUCTURE OF PORIN FROM RHODOPSEUDOMONAS BLASTICA AND COMPARISON WITH THE PORIN FROM RHODOBACTER CAPSULATUS

Released:
DOI: 10.2210/pdb1prn/pdb
PDB entry 1prn coloured by chain, front view.
PDB entry 1prn coloured by chain, side view.
PDB entry 1prn coloured by chain, top view.
Source organism: Fuscovulum blasticum
Primary publication:
Refined structure of the porin from Rhodopseudomonas blastica. Comparison with the porin from Rhodobacter capsulatus.
Kreusch A, Schulz GE
J Mol Biol 243 891-905 (1994)
PMID: 7525973

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-153944 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Porin Chain: A
Molecule details ›
Chain: A
Length: 289 amino acids
Theoretical weight: 30.61 KDa
Source organism: Fuscovulum blasticum
Expression system: Not provided
UniProt:
  • Canonical: P39767 (Residues: 1-289; Coverage: 100%)
Gene name: opmA
Sequence domains: Gram-negative porin
Structure domains: Porin

Ligands and Environments

1 bound ligand:
Ligand C8E 3 x C8E
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: R3
Unit cell:
a: 104.3Å b: 104.3Å c: 124.6Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.176 0.176 not available
Expression system: Not provided

Quick links

Citations

11 review citations

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

31 mentions without citation

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