› 6sar

X-ray diffraction
2.18Å resolution

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-159194 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-barrel assembly-enhancing protease Chain: A
Molecule details ›
Chain: A
Length: 487 amino acids
Theoretical weight: 53.96 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P66948 (Residues: 1-487; Coverage: 100%)
Gene names: JW2479, b2494, bepA, yfgC
Sequence domains:

Ligands and Environments

2 bound ligands:
Ligand ZN 1 x ZN
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I03
Spacegroup: P212121
Unit cell:
a: 53.12Å b: 77.02Å c: 124.6Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.178 0.176 0.201
Expression system: Escherichia coli

Quick links

Citations

3 citation in other articles

Reversible autoinhibitory regulation of Escherichia coli metallopeptidase BepA for selective β-barrel protein degradation.
Daimon et al. (2020)
2 more

3 mentions without citation

α-Helices in the Type III Secretion Effectors: A Prevalent Feature with Versatile Roles.
Gazi et al. (2021)
2 more