Research workbench
BEST1 open state W287F mutant, calcium-bound
Analyse BEST1 open state W287F mutant, calcium-bound in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6N25
- Type
- protein
- Length
- 1,690 residues
- Chains
- 5
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Bestrophin homolog
- UniProt
- E1C3A0
- Ligands
- CA
- Pockets
- 20 · best druggability 0.67
Structure
electron microscopy · 1 distinct chain · 66% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E | Bestrophin homolog | protein | 338 | 66% helix, 1% strand | E1C3A0 |
Ligands and binding sites
- CA · Calcium ion · metal · 5 copies · chains A, E, 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, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 600 | 0.67 | 0.77 | 48 | empty |
| 2 | 214 | 0.67 | 0.85 | 24 | empty |
| 3 | 229 | 0.66 | 0.84 | 23 | empty |
| 4 | 218 | 0.66 | 0.84 | 24 | empty |
| 5 | 238 | 0.66 | 0.83 | 24 | empty |
Interfaces
5 interfaces between chains.
- B–C · 4426 Ų buried · 33 hydrogen bonds · protein-protein
- A–B · 4423 Ų buried · 37 hydrogen bonds · protein-protein
- A–E · 4417 Ų buried · 30 hydrogen bonds · protein-protein
- C–D · 4416 Ų buried · 31 hydrogen bonds · protein-protein
- D–E · 4407 Ų buried · 30 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 5 disulfide (disulfide).
Compared structures
- 6N25 · BEST1 open state W287F mutant, calcium-bound · 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 6N25 · PDBe 6N25 · UniProt E1C3A0
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