› 5prn

X-ray diffraction
2Å resolution

E1M, Y96W, S119W MUTANT OF RH. BLASTICA PORIN

Released:
DOI: 10.2210/pdb5prn/pdb
PDB entry 5prn coloured by chain, front view.
PDB entry 5prn coloured by chain, side view.
PDB entry 5prn coloured by chain, top view.
Source organism: Fuscovulum blasticum
Primary publication:
Porin mutants with new channel properties.
Schmid B, Maveyraud L, Krömer M, Schulz GE
Protein Sci 7 1603-11 (1998)
PMID: 9684893

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: 30.73 KDa
Source organism: Fuscovulum blasticum
Expression system: Escherichia coli
UniProt:
  • Canonical: P39767 (Residues: 2-289; 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
X-ray source: RIGAKU RUH2R
Spacegroup: R3
Unit cell:
a: 104.6Å b: 104.6Å c: 124.66Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.163 0.163 0.188
Expression system: Escherichia coli

Quick links

Citations

4 review citations

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

1 mention without citation

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