PDBe 1i78

X-ray diffraction
2.6Å resolution

CRYSTAL STRUCTURE OF OUTER MEMBRANE PROTEASE OMPT FROM ESCHERICHIA COLI

Released:

Function and Biology Details

Reaction catalysed:
Has a virtual requirement for Arg in the P1 position and a slightly less stringent preference for this residue in the P1' position, which can also contain Lys, Gly or Val. 
Biological process:
Cellular component:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protease 7 Chains: A, B
Molecule details ›
Chains: A, B
Length: 297 amino acids
Theoretical weight: 33.5 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P09169 (Residues: 21-317; Coverage: 100%)
Gene names: JW0554, b0565, ompT
Sequence domains: Omptin family
Structure domains: OMPT-like

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P3221
Unit cell:
a: 98.389Å b: 98.389Å c: 165.695Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.238 0.238 0.28
Expression system: Escherichia coli BL21(DE3)