› 4ey0

X-ray diffraction
2.8Å resolution

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-148516 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 246 amino acids
Theoretical weight: 28.63 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P19174 (Residues: 545-790; Coverage: 19%)
Gene names: PLC1, PLCG1
Sequence domains: SH2 domain
Structure domains: SH2 domain

Ligands and Environments

No bound ligands
1 modified residue:
Ligand PTR 4 x PTR

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: P1
Unit cell:
a: 54.9Å b: 59.2Å c: 79.2Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.199 0.197 0.242
Expression system: Escherichia coli

Quick links

Citations

12 review citations

Dysfunction of phospholipase Cγ in immune disorders and cancer.
Koss et al. (2014)
11 more

8 mentions without citation

Conformational switches that control the TEC kinase - PLCγ signaling axis.
Lowe et al. (2022)
7 more