Research workbench
Structure of calcium-bound MTMEM16A chloride channel at 3.75 a resolution
Analyse Structure of calcium-bound MTMEM16A chloride channel at 3.75 a resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5OYB
- Type
- protein
- Length
- 1,436 residues
- Chains
- 2
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Anoctamin-1
- UniProt
- Q8BHY3
- Ligands
- CA
- Pockets
- 20 · best druggability 0.83
Structure
electron microscopy · 1 distinct chain · 55% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Anoctamin-1 | protein | 718 | 55% helix, 5% strand | Q8BHY3 |
Ligands and binding sites
- CA · Calcium ion · metal · 4 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, 11 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 713 | 0.83 | 0.87 | 59 | empty |
| 2 | 736 | 0.82 | 0.85 | 60 | empty |
| 3 | 1187 | 0.78 | 0.80 | 98 | empty |
| 4 | 1184 | 0.78 | 0.79 | 93 | empty |
| 5 | 811 | 0.75 | 0.79 | 57 | empty |
Interfaces
1 interface between chains.
- A–B · 818 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 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 Q8BHY3
- Elsewhere: RCSB PDB 5OYB · PDBe 5OYB · UniProt Q8BHY3
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