Research workbench
Bestrophin-2 CA2+-bound state (5 mm CA2+)
Analyse Bestrophin-2 CA2+-bound state (5 mm CA2+) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6VX7
- Type
- protein
- Length
- 1,830 residues
- Chains
- 5
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Bestrophin
- UniProt
- E1BF86
- Ligands
- CA, CL
- Pockets
- 20 · best druggability 0.80
Structure
electron microscopy · 1 distinct chain · 63% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| C, A, B, E, D | Bestrophin | protein | 366 | 63% helix, 1% strand | E1BF86 |
Ligands and binding sites
- CA · Calcium ion · metal · 5 copies · chains C, B, A, E, D
- CL · Chloride ion · ion · chains C, A, B, E, 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, 16 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 916 | 0.80 | 0.82 | 72 | empty |
| 2 | 629 | 0.76 | 0.82 | 92 | CL |
| 3 | 61 | 0.73 | 0.98 | 16 | empty |
| 4 | 59 | 0.72 | 0.98 | 16 | empty |
| 5 | 53 | 0.72 | 0.98 | 16 | empty |
Interfaces
10 interfaces between chains.
- A–B · 5155 Ų buried · 45 hydrogen bonds · protein-protein
- C–B · 5144 Ų buried · 45 hydrogen bonds · protein-protein
- E–D · 5137 Ų buried · 43 hydrogen bonds · protein-protein
- A–E · 5136 Ų buried · 40 hydrogen bonds · protein-protein
- C–D · 5130 Ų buried · 46 hydrogen bonds · protein-protein
Compared structures
- 6VX7 · bestrophin-2 Ca2+-bound state (5 mM Ca2+) · the same entry in another collection · chain C against C, 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 E1BF86
- Elsewhere: RCSB PDB 6VX7 · PDBe 6VX7 · UniProt E1BF86
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.