MolNFT v1 · #33351 · protein
A pharmacological MAP of the PI3-K family defines a role for P110ALPHA in signaling: the structure of complex of phosphoinositide 3-kinase gamma with inhibitor pik-90
2CHX · Phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic…: “A pharmacological MAP of the PI3-K family defines a role for P110ALPHA in signaling: the structure of complex…”. X-ray diffraction, 1 ligand (090), 14 pockets (best…
- PDB
- 2CHX
- Type
- protein
- Length
- 842 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit gamma isoform
- EC
- 2.7.1.137, 2.7.1.153
- UniProt
- P48736
- Ligands
- 090
- Pockets
- 14 · best druggability 0.81
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit gamma isoform (EC 2.7.1.137, 2.7.1.153) | protein | 842 | 44% helix, 17% strand | P48736 |
Ligands and binding sites
- 090 · N-(2,3-dihydro-7,8-dimethoxyimidazo[1,2-C] quinazolin-5-yl)nicotinamide · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
14 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1162 | 0.81 | 0.82 | 78 | empty |
| 2 | 99 | 0.77 | 0.97 | 35 | empty |
| 3 | 377 | 0.68 | 0.81 | 41 | 090 |
| 4 | 564 | 0.68 | 0.78 | 77 | empty |
| 5 | 194 | 0.60 | 0.82 | 32 | empty |
Compared structures
- 2CHX · A pharmacological map of the PI3-K family defines a role for p110alpha in signaling: The… · the same entry in another collection · chain A against A, TM-score 1.00
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 P48736
- Elsewhere: RCSB PDB 2CHX · PDBe 2CHX · UniProt P48736
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