Research workbench
Structure and activity of SLAC1 channels for stomatal signaling in leaves
Analyse Structure and activity of SLAC1 channels for stomatal signaling in leaves in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7EN0
- Type
- protein
- Length
- 939 residues
- Chains
- 3
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Slow anion channel 1
- UniProt
- A0A0Q3IDG7
- Ligands
- PLC, SPH
- Pockets
- 19 · best druggability 0.83
Structure
electron microscopy · 1 distinct chain · 72% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Slow anion channel 1 | protein | 313 | 72% helix, 0% strand | A0A0Q3IDG7 |
Ligands and binding sites
- PLC · Diundecyl phosphatidyl choline · ligand · 3 copies · chains A, C, B
- SPH · Sphingosine · ligand · 3 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
19 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 654 | 0.83 | 0.87 | 42 | SPH |
| 2 | 225 | 0.56 | 0.78 | 38 | empty |
| 3 | 215 | 0.54 | 0.77 | 34 | empty |
| 4 | 195 | 0.53 | 0.77 | 39 | empty |
| 5 | 210 | 0.52 | 0.76 | 23 | PLC |
Interfaces
3 interfaces between chains.
- A–C · 1109 Ų buried · 8 hydrogen bonds · protein-protein
- A–B · 1108 Ų buried · 8 hydrogen bonds · protein-protein
- B–C · 1103 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 7EN0 · Structure and Activity of SLAC1 Channels for Stomatal Signaling in Leaves · the same entry in another collection · chain A against A, TM-score 1.00
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 A0A0Q3IDG7
- Elsewhere: RCSB PDB 7EN0 · PDBe 7EN0 · UniProt A0A0Q3IDG7
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