Research workbench
Structure of autoinhibited AKT1 reveals mechanism of PIP3-mediated activation
Analyse Structure of autoinhibited AKT1 reveals mechanism of PIP3-mediated activation in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7APJ
- Type
- protein
- Length
- 502 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Rac-alpha SERINE/THREONINE-protein KINASE,NON-specific SERINE/THREONINE protein…
- EC
- 2.7.11.1
- UniProt
- P31749, M4MD44
- Pockets
- 6 · best druggability 0.52
Structure
x-ray diffraction · 2 distinct chains · 27% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Rac-alpha SERINE/THREONINE-protein KINASE,NON-specific SERINE/THREONINE protein KINASE,RAC-alpha SERINE/THREONINE-protein kinase (EC 2.7.11.1) | protein | 385 | 32% helix, 24% strand | P31749, M4MD44 |
| B | NB41 | protein | 117 | 12% helix, 45% strand | — |
Pockets
6 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 130 | 0.52 | 0.80 | 17 | empty |
| 2 | 142 | 0.45 | 0.77 | 22 | empty |
| 3 | 61 | 0.43 | 0.82 | 15 | empty |
| 4 | 64 | 0.31 | 0.75 | 13 | empty |
| 5 | 55 | 0.31 | 0.76 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 762 Ų buried · 10 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 7APJ · Structure of autoinhibited Akt1 reveals mechanism of PIP3-mediated activation · the same entry in another collection · chain A against A, TM-score 1.00
- P31749 · AlphaFold monomer V2.0 prediction for rac-alpha SERINE/THREONINE- protein kinase (P31749) · a predicted model of the same protein · chain A against A, TM-score 0.80
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 P31749
- Every structure of UniProt M4MD44
- Elsewhere: RCSB PDB 7APJ · PDBe 7APJ · UniProt P31749 · UniProt M4MD44
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