Research workbench
Cryo-EM structure of CA2+-free HSSLO1 channel
Analyse Cryo-EM structure of CA2+-free HSSLO1 channel in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6V3G
- Type
- protein
- Length
- 3,580 residues
- Chains
- 4
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Calcium-activated potassium channel subunit alpha-1
- UniProt
- Q12791
- Pockets
- 20 · best druggability 0.78
Structure
electron microscopy · 1 distinct chain · 41% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B, A, C, D | Calcium-activated potassium channel subunit alpha-1 | protein | 895 | 41% helix, 13% strand | Q12791 |
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1151 | 0.78 | 0.80 | 134 | empty |
| 2 | 107 | 0.78 | 0.98 | 19 | empty |
| 3 | 107 | 0.78 | 0.97 | 21 | empty |
| 4 | 109 | 0.78 | 0.97 | 22 | empty |
| 5 | 102 | 0.77 | 0.97 | 20 | empty |
Interfaces
6 interfaces between chains.
- A–D · 1946 Ų buried · 15 hydrogen bonds · protein-protein
- C–D · 1942 Ų buried · 15 hydrogen bonds · protein-protein
- B–C · 1939 Ų buried · 15 hydrogen bonds · protein-protein
- B–A · 1936 Ų buried · 15 hydrogen bonds · protein-protein
- A–C · 49 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 6V3G · Cryo-EM structure of Ca2+-free hsSlo1 channel · the same entry in another collection · chain D against D, TM-score 1.00
- Q12791 · AlphaFold monomer V2.0 prediction for calcium-activated potassium channel subunit alpha-1… · a predicted model of the same protein · chain B against A, TM-score 0.94
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 Q12791
- Elsewhere: RCSB PDB 6V3G · PDBe 6V3G · UniProt Q12791
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