› 8gud

Electron Microscopy
2.62Å resolution

Cryo-EM structure of cancer-specific PI3Kalpha mutant E545K in complex with BYL-719

Released:
DOI: 10.2210/pdb8gud/pdb
PDB entry 8gud coloured by chain, front view.
PDB entry 8gud coloured by chain, side view.
PDB entry 8gud coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Cryo-EM structures of cancer-specific helical and kinase domain mutations of PI3Kα.
Liu X, Zhou Q, Hart JR, Xu Y, Yang S, Yang D, Vogt PK, Wang MW
OpenAccess logo Proc Natl Acad Sci U S A 119 e2215621119 (2022)
PMID: 36343266
Related structures: EMD-34273

Function and Biology Details

Reactions catalysed: 
ATP + 1-phosphatidyl-1D-myo-inositol = ADP + 1-phosphatidyl-1D-myo-inositol 3-phosphate
ATP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate = ADP + 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate
ATP + a protein = ADP + a phosphoprotein
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-154615 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha isoform Chain: A
Molecule details ›
Chain: A
Length: 1096 amino acids
Theoretical weight: 127.82 KDa
Source organism: Homo sapiens
Expression system: Trichoplusia ni
UniProt:
  • Canonical: P42336 (Residues: 1-1068; Coverage: 100%)
Gene name: PIK3CA
Sequence domains:

Ligands and Environments

1 bound ligand:
Ligand 1LT 1 x 1LT
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 2.62Å
Relevant EMDB volumes: EMD-34273
Expression system: Trichoplusia ni

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Citations

2 review citations

Recent Advances in the Knowledge of the Mechanisms of Leptin Physiology and Actions in Neurological and Metabolic Pathologies.
Casado et al. (2023)
1 more