Research workbench
Cryo-EM structure of ATSLAC1 S59A mutant
Analyse Cryo-EM structure of ATSLAC1 S59A mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7WNQ
- Type
- protein
- Length
- 1,104 residues
- Chains
- 3
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Guard cell S-type anion channel SLAC1
- UniProt
- Q9LD83
- Pockets
- 20 · best druggability 0.83
Structure
electron microscopy · 1 distinct chain · 64% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Guard cell S-type anion channel SLAC1 | protein | 368 | 64% helix, 2% strand | Q9LD83 |
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 | 856 | 0.83 | 0.84 | 62 | empty |
| 2 | 559 | 0.73 | 0.80 | 54 | empty |
| 3 | 559 | 0.72 | 0.80 | 57 | empty |
| 4 | 556 | 0.72 | 0.80 | 64 | empty |
| 5 | 51 | 0.66 | 0.96 | 15 | empty |
Interfaces
3 interfaces between chains.
- A–C · 1233 Ų buried · 9 hydrogen bonds · protein-protein
- A–B · 1222 Ų buried · 8 hydrogen bonds · protein-protein
- B–C · 1217 Ų buried · 8 hydrogen bonds · protein-protein
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 Q9LD83
- Elsewhere: RCSB PDB 7WNQ · PDBe 7WNQ · UniProt Q9LD83
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