Research workbench
Cryoem structure of calcium-bound human TMEM16K / anoctamin 10 in detergent (2MM CA2+, closed form)
Analyse Cryoem structure of calcium-bound human TMEM16K / anoctamin 10 in detergent… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6R7X
- Type
- protein
- Length
- 1,258 residues
- Chains
- 2
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Anoctamin-10
- UniProt
- Q9NW15
- Ligands
- UMQ, PC1, CA
- Pockets
- 20 · best druggability 0.77
Structure
electron microscopy · 1 distinct chain · 60% helix, 7% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Anoctamin-10 | protein | 629 | 60% helix, 7% strand | Q9NW15 |
Ligands and binding sites
- UMQ · Undecyl-maltoside · ligand · 20 copies · chains A, B
- PC1 · 1,2-diacyl-sn-glycero-3-phosphocholine · ligand · 2 copies · chains A, B
- CA · Calcium ion · metal · 6 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, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 896 | 0.77 | 0.80 | 100 | empty |
| 2 | 1162 | 0.75 | 0.77 | 97 | empty |
| 3 | 297 | 0.70 | 0.84 | 31 | empty |
| 4 | 313 | 0.69 | 0.83 | 35 | empty |
| 5 | 330 | 0.61 | 0.78 | 39 | UMQ |
Interfaces
1 interface between chains.
- A–B · 1301 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 6R7X · CryoEM structure of calcium-bound human TMEM16K / Anoctamin 10 in detergent (2mM Ca2+… · the same entry in another collection · chain A against A, TM-score 1.00
- Q9NW15 · AlphaFold monomer V2.0 prediction for anoctamin-10 (Q9NW15) · a predicted model of the same protein · chain B against A, TM-score 0.93
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 Q9NW15
- Elsewhere: RCSB PDB 6R7X · PDBe 6R7X · UniProt Q9NW15
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