3v16

X-ray diffraction
2.05Å resolution

An intramolecular pi-cation latch in phosphatidylinositol-specific phospholipase C from S.aureus controls substrate access to the active site

Released:

Function and Biology Details

Reaction catalysed:
1-phosphatidyl-1D-myo-inositol = 1D-myo-inositol 1,2-cyclic phosphate + 1,2-diacyl-sn-glycerol
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-155335 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
1-phosphatidylinositol phosphodiesterase Chain: A
Molecule details ›
Chain: A
Length: 303 amino acids
Theoretical weight: 34.28 KDa
Source organism: Staphylococcus aureus subsp. aureus str. Newman
UniProt:
  • Canonical: P45723 (Residues: 11-312; Coverage: 100%)
Gene names: NWMN_0041, plc
Sequence domains: Phosphatidylinositol-specific phospholipase C, X domain
Structure domains: Phosphatidylinositol (PI) phosphodiesterase

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P212121
Unit cell:
a: 104.161Å b: 43.607Å c: 62.218Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.158 0.156 0.213