Research workbench
Cryo-EM structure of TMEM16F in digitonin with calcium bound
Analyse Cryo-EM structure of TMEM16F in digitonin with calcium bound in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6P46
- Type
- protein
- Length
- 1,380 residues
- Chains
- 2
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Anoctamin-6
- UniProt
- Q6P9J9
- Ligands
- CA
- Pockets
- 20 · best druggability 0.77
Structure
electron microscopy · 1 distinct chain · 52% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Anoctamin-6 | protein | 690 | 52% helix, 2% strand | Q6P9J9 |
Ligands and binding sites
- CA · Calcium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 15 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1033 | 0.77 | 0.79 | 95 | empty |
| 2 | 983 | 0.77 | 0.79 | 83 | empty |
| 3 | 181 | 0.72 | 0.89 | 43 | empty |
| 4 | 358 | 0.72 | 0.83 | 56 | empty |
| 5 | 303 | 0.71 | 0.84 | 45 | empty |
Interfaces
1 interface between chains.
- A–B · 878 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide (disulfide).
Compared structures
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 Q6P9J9
- Elsewhere: RCSB PDB 6P46 · PDBe 6P46 · UniProt Q6P9J9
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