› 3kk7

X-ray diffraction
2.46Å resolution

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-183638 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
MACPF domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 541 amino acids
Theoretical weight: 62.01 KDa
Source organism: Bacteroides thetaiotaomicron VPI-5482
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8A267 (Residues: 19-558; Coverage: 97%)
Gene name: BT_3439
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand CL 1 x CL
Ligand EDO 3 x EDO
Ligand MPD 1 x MPD
1 modified residue:
Ligand MSE 22 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-2
Spacegroup: P212121
Unit cell:
a: 78.4Å b: 127.2Å c: 138.25Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.211 0.209 0.252
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Pore-forming toxins: ancient, but never really out of fashion.
Dal Peraro et al. (2016)
3 more

7 mentions without citation

Packing a punch: the mechanism of pore formation by cholesterol dependent cytolysins and membrane attack complex/perforin-like proteins.
Dunstone et al. (2012)
6 more