Research workbench
Cryo-EM structure of the Potassium channel AKT1 mutant from Arabidopsis thaliana
Analyse Cryo-EM structure of the Potassium channel AKT1 mutant from Arabidopsis thaliana in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7FCV
- Type
- protein
- Length
- 1,848 residues
- Chains
- 4
- Method
- electron microscopy
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.9
- Source
- Arabidopsis thaliana
- Molecule
- Potassium channel AKT1
- UniProt
- Q38998
- Ligands
- PTY, K
- Pockets
- 20 · best druggability 0.81
Structure
electron microscopy · resolution 2.9 · 1 distinct chain · 56% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Potassium channel AKT1 | protein | 462 | 56% helix, 10% strand | Q38998 |
Ligands and binding sites
- PTY · Phosphatidylethanolamine · ligand · 4 copies · chains A, B, C, D
- K · Potassium ion · metal · 3 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 697 | 0.81 | 0.84 | 87 | empty |
| 2 | 782 | 0.72 | 0.77 | 53 | empty |
| 3 | 751 | 0.70 | 0.76 | 48 | empty |
| 4 | 464 | 0.69 | 0.80 | 65 | empty |
| 5 | 706 | 0.69 | 0.76 | 45 | empty |
Interfaces
6 interfaces between chains.
- B–C · 2810 Ų buried · 13 hydrogen bonds · protein-protein
- A–B · 2786 Ų buried · 14 hydrogen bonds · protein-protein
- C–D · 2767 Ų buried · 16 hydrogen bonds · protein-protein
- A–D · 2735 Ų buried · 14 hydrogen bonds · protein-protein
- A–C · 64 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- Q38998 · AlphaFold monomer V2.0 prediction for potassium channel AKT1 (Q38998) · a predicted model of the same protein · chain C 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 Q38998
- Elsewhere: RCSB PDB 7FCV · PDBe 7FCV · UniProt Q38998
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