6pbc

X-ray diffraction
2.46Å resolution

Structural basis for the activation of PLC-gamma isozymes by phosphorylation and cancer-associated mutations

Released:

Function and Biology Details

Reaction catalysed:
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H(2)O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-246281 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma; 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1 Chain: A
Molecule details ›
Chain: A
Length: 1176 amino acids
Theoretical weight: 135.96 KDa
Source organism: Rattus norvegicus
Expression system: Trichoplusia ni
UniProt:
  • Canonical: P10686 (Residues: 21-200, 791-1215; Coverage: 47%)
  • Canonical: G3V845 (Residues: 201-765; Coverage: 44%)
Gene name: Plcg1
Sequence domains:

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-BM
Spacegroup: P212121
Unit cell:
a: 70.766Å b: 82.441Å c: 228.318Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.205 0.202 0.245
Expression system: Trichoplusia ni