MolNFT v1 · #157517 · protein
BEST1 in a calcium-bound inactivated state
6N23 · Bestrophin homolog: “BEST1 in a calcium-bound inactivated state”. Electron microscopy, 1 ligand (CA), 20 pockets (best druggability 0.73). MolNFT v1 #157517 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6N23
- Type
- protein
- Length
- 1,815 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 0.73
Structure
electron microscopy · 1 distinct chain · 60% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E | Bestrophin homolog | protein | 363 | 60% helix, 0% 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, 18 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 71 | 0.73 | 0.97 | 16 | empty |
| 2 | 899 | 0.73 | 0.77 | 80 | empty |
| 3 | 68 | 0.73 | 0.97 | 15 | empty |
| 4 | 68 | 0.72 | 0.97 | 15 | empty |
| 5 | 74 | 0.71 | 0.95 | 16 | empty |
Interfaces
10 interfaces between chains.
- D–E · 5289 Ų buried · 41 hydrogen bonds · protein-protein
- A–B · 5280 Ų buried · 38 hydrogen bonds · protein-protein
- C–D · 5275 Ų buried · 39 hydrogen bonds · protein-protein
- A–E · 5274 Ų buried · 40 hydrogen bonds · protein-protein
- B–C · 5265 Ų buried · 37 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 5 disulfide (disulfide).
Compared structures
- 6N23 · BEST1 in a calcium-bound inactivated 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 6N23 · PDBe 6N23 · UniProt E1C3A0
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