Research workbench
Cryo-EM structure of calcium-bound TMEM16F in nanodisc with supplement of PIP2 in CL1
Analyse Cryo-EM structure of calcium-bound TMEM16F in nanodisc with supplement of PIP2… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6P48
- Type
- protein
- Length
- 1,208 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 0.72
Structure
electron microscopy · 1 distinct chain · 53% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Anoctamin-6 | protein | 604 | 53% 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, 16 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 488 | 0.72 | 0.81 | 57 | empty |
| 2 | 544 | 0.72 | 0.80 | 60 | empty |
| 3 | 770 | 0.72 | 0.77 | 57 | empty |
| 4 | 718 | 0.71 | 0.77 | 57 | empty |
| 5 | 329 | 0.70 | 0.83 | 43 | empty |
Interfaces
1 interface between chains.
- A–B · 906 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 disulfide (disulfide).
Compared structures
- 6P48 · Cryo-EM structure of calcium-bound TMEM16F in nanodisc with supplement of PIP2 in Cl1 · the same entry in another collection · chain A against A, TM-score 1.00
- Q6P9J9 · AlphaFold monomer V2.0 prediction for anoctamin-6 (Q6P9J9) · a predicted model of the same protein · chain B against A, TM-score 0.90
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 6P48 · PDBe 6P48 · UniProt Q6P9J9
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