Research workbench
Crystal structure of the PDK1 pleckstrin homology (pH) domain bound to DIC4-phosphatidylinositol (3,4,5)- trisphosphate
Analyse Crystal structure of the PDK1 pleckstrin homology (pH) domain bound to… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1W1G
- Type
- protein
- Length
- 143 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 3-phosphoinositide dependent protein kinase-1
- EC
- 2.7.1.37
- UniProt
- O15530
- Ligands
- 4PT
- Pockets
- 2 · best druggability 0.44
Structure
x-ray diffraction · 1 distinct chain · 26% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 3-phosphoinositide dependent protein kinase-1 (EC 2.7.1.37) | protein | 143 | 26% helix, 41% strand | O15530 |
Ligands and binding sites
- 4PT · (2R)-3-{[(S)-{[(2S,3R,5S,6S)-2,6-dihydroxy-3,4,5-tris(phosphonooxy)cyclohexyl]oxy}(hydroxy) phosphoryl]oxy}-2-(1-hydroxybutoxy)propyl butyrate · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 75 | 0.44 | 0.81 | 17 | empty |
| 2 | 79 | 0.36 | 0.76 | 12 | empty |
Compared structures
- 1W1G · Crystal Structure of the PDK1 Pleckstrin Homology (PH) domain bound to… · the same entry in another collection · chain A against A, TM-score 1.00
- O15530 · AlphaFold monomer V2.0 prediction for 3-phosphoinositide-dependent protein kinase 1… · a predicted model of the same protein · chain A against A, TM-score 0.92
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 O15530
- Elsewhere: RCSB PDB 1W1G · PDBe 1W1G · UniProt O15530
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