MolNFT v1 · #5141 · protein
Structural insights into phoshoinositide 3-kinase enzymatic mechanism and signalling
1E8X · Phosphatidylinositol 3-kinase catalytic subunit: “Structural insights into phoshoinositide 3-kinase enzymatic mechanism and signalling”. X-ray diffraction, 2 ligands (ATP, LU), 15 pockets (best druggability 0.82). MolNFT v1 #5141 on…
- PDB
- 1E8X
- Type
- protein
- Length
- 841 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phosphatidylinositol 3-kinase catalytic subunit
- EC
- 2.7.1.137
- UniProt
- O02697
- Ligands
- ATP, LU
- Pockets
- 15 · best druggability 0.82
Structure
x-ray diffraction · 1 distinct chain · 45% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphatidylinositol 3-kinase catalytic subunit (EC 2.7.1.137) | protein | 841 | 45% helix, 17% strand | O02697 |
Ligands and binding sites
- ATP · Adenosine-5'-triphosphate · ligand · chains A
- LU · Lutetium (III) ion · metal · 9 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
15 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1119 | 0.82 | 0.83 | 75 | empty |
| 2 | 52 | 0.70 | 0.98 | 17 | empty |
| 3 | 280 | 0.68 | 0.83 | 36 | empty |
| 4 | 435 | 0.68 | 0.79 | 50 | ATP, LU |
| 5 | 172 | 0.58 | 0.82 | 32 | empty |
Compared structures
- 1E8X · Structural insights into phoshoinositide 3-kinase enzymatic mechanism and signalling · the same entry in another collection · chain A against A, TM-score 1.00
- O02697 · AlphaFold monomer V2.0 prediction for phosphatidylinositol 4,5-bisphosphate 3-kinase… · a predicted model of the same protein · chain A against A, TM-score 0.97
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt O02697
- Elsewhere: RCSB PDB 1E8X · PDBe 1E8X · UniProt O02697
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