Research workbench
Crystal structure of human AKT2 in complex with GSK690693
Analyse Crystal structure of human AKT2 in complex with GSK690693 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3D0E
- Type
- protein
- Length
- 648 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Rac-beta SERINE/THREONINE-protein kinase
- EC
- 2.7.11.1
- UniProt
- P31751
- Ligands
- G93
- Pockets
- 10 · best druggability 0.80
Structure
x-ray diffraction · 1 distinct chain · 35% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Rac-beta SERINE/THREONINE-protein kinase (EC 2.7.11.1) | protein | 324 | 35% helix, 15% strand | P31751 |
Ligands and binding sites
- G93 · 4-{2-(4-amino-1,2,5-oxadiazol-3-yl)-1-ethyl-7-[(3S)-piperidin-3-ylmethoxy]-1H-imidazo[4,5-c]pyridin-4-yl}-2-methylbut-3-yn-2-ol · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1192 | 0.80 | 0.81 | 85 | G93 |
| 2 | 495 | 0.75 | 0.83 | 61 | G93 |
| 3 | 352 | 0.60 | 0.77 | 40 | empty |
| 4 | 113 | 0.47 | 0.79 | 20 | empty |
| 5 | 159 | 0.40 | 0.73 | 24 | empty |
Interfaces
1 interface between chains.
- A–B · 565 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 modified (phosphorylation).
Compared structures
- 3D0E · Crystal structure of human Akt2 in complex with GSK690693 · the same entry in another collection · chain A against A, TM-score 1.00
- P31751 · AlphaFold monomer V2.0 prediction for rac-beta SERINE/THREONINE- protein kinase (P31751) · 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 P31751
- Elsewhere: RCSB PDB 3D0E · PDBe 3D0E · UniProt P31751
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