› 1olp

X-ray diffraction
2.5Å resolution

Function and Biology Details

Reaction catalysed: 
A phosphatidylcholine + H(2)O = 1,2-diacyl-sn-glycerol + phosphocholine
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-184497 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phospholipase C Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 370 amino acids
Theoretical weight: 42.75 KDa
Source organism: Clostridium sardiniense
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8GCY3 (Residues: 29-398; Coverage: 100%)
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand CA 8 x CA
Ligand ZN 12 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P21212
Unit cell:
a: 92.956Å b: 193.592Å c: 92.686Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.181 0.178 0.237
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Membrane-Binding Mechanism of Clostridium perfringens Alpha-Toxin.
Oda et al. (2015)
13 other articles

5 mentions without citation

The role of hydrophobic interactions in positioning of peripheral proteins in membranes.
Lomize et al. (2007)
4 more