Research workbench
MPI3KD in complex with 5D
Analyse MPI3KD in complex with 5D in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5T27
- Type
- protein
- Length
- 819 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
- 74F
- Pockets
- 8 · best druggability 0.81
Structure
x-ray diffraction · 1 distinct chain · 47% helix, 18% 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 | 819 | 47% helix, 18% strand | O35904 |
Ligands and binding sites
- 74F · 3-(benzotriazol-1-yl)-5-[1-methyl-5-[(1~{S})-1-morpholin-4-ylethyl]-1,2,4-triazol-3-yl]pyrazin-2-amine · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1179 | 0.81 | 0.82 | 90 | empty |
| 2 | 856 | 0.72 | 0.77 | 81 | empty |
| 3 | 292 | 0.68 | 0.83 | 40 | empty |
| 4 | 117 | 0.63 | 0.87 | 30 | empty |
| 5 | 256 | 0.61 | 0.80 | 32 | 74F |
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 5T27 · PDBe 5T27 · UniProt O35904
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