Research workbench
MPI3KD in complex with AZ3
Analyse MPI3KD in complex with AZ3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6GY0
- Type
- protein
- Length
- 822 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit delta isoform
- EC
- 2.7.1.153
- UniProt
- O35904
- Ligands
- FGE
- Pockets
- 13 · best druggability 0.81
Structure
x-ray diffraction · 1 distinct chain · 47% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit delta isoform (EC 2.7.1.153) | protein | 822 | 47% helix, 17% strand | O35904 |
Ligands and binding sites
- FGE · ~{N}-[4-methyl-5-(1-oxidanylidene-7-sulfamoyl-isoindol-5-yl)-1,3-thiazol-2-yl]ethanamide · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
13 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1114 | 0.81 | 0.82 | 88 | empty |
| 2 | 310 | 0.68 | 0.82 | 40 | empty |
| 3 | 114 | 0.62 | 0.86 | 23 | empty |
| 4 | 364 | 0.61 | 0.77 | 35 | empty |
| 5 | 292 | 0.61 | 0.79 | 36 | FGE |
Compared structures
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 O35904
- Elsewhere: RCSB PDB 6GY0 · PDBe 6GY0 · UniProt O35904
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.