Research workbench
BEST1 calcium-bound open state
Analyse BEST1 calcium-bound open state in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6N28
- Type
- protein
- Length
- 1,690 residues
- Chains
- 5
- Method
- electron microscopy
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.9
- Source
- Gallus gallus
- Molecule
- Bestrophin homolog
- UniProt
- E1C3A0
- Ligands
- CA
- Pockets
- 20 · best druggability 0.67
Structure
electron microscopy · resolution 2.9 · 1 distinct chain · 66% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E | Bestrophin homolog | protein | 338 | 66% helix, 0% strand | E1C3A0 |
Ligands and binding sites
- CA · Calcium ion · metal · 5 copies · chains A, B, C, D, E
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 216 | 0.67 | 0.85 | 23 | empty |
| 2 | 605 | 0.67 | 0.77 | 47 | empty |
| 3 | 225 | 0.67 | 0.84 | 25 | empty |
| 4 | 219 | 0.66 | 0.84 | 22 | empty |
| 5 | 225 | 0.65 | 0.84 | 22 | empty |
Interfaces
5 interfaces between chains.
- A–E · 4444 Ų buried · 35 hydrogen bonds · protein-protein
- A–B · 4441 Ų buried · 35 hydrogen bonds · protein-protein
- D–E · 4440 Ų buried · 36 hydrogen bonds · protein-protein
- B–C · 4440 Ų buried · 35 hydrogen bonds · protein-protein
- C–D · 4437 Ų buried · 36 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 5 disulfide (disulfide).
Compared structures
- 6N28 · BEST1 calcium-bound open state · the same entry in another collection · chain A against A, TM-score 1.00
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 E1C3A0
- Elsewhere: RCSB PDB 6N28 · PDBe 6N28 · UniProt E1C3A0
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