MolNFT v1 · #157863 · protein
Human bk channel reconstituted into liposomes
6ND0 · Calcium-activated potassium channel subunit alpha-1: “Human bk channel reconstituted into liposomes”. Electron microscopy, 20 pockets (best druggability 0.81). MolNFT v1 #157863 on GenesisL1: 3D structure, binding sites and pockets…
- PDB
- 6ND0
- Type
- protein
- Length
- 2,908 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 0.81
Structure
electron microscopy · 1 distinct chain · 35% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Calcium-activated potassium channel subunit alpha-1 | protein | 727 | 35% helix, 16% 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 | 929 | 0.81 | 0.82 | 116 | empty |
| 2 | 946 | 0.80 | 0.82 | 108 | empty |
| 3 | 185 | 0.78 | 0.93 | 26 | empty |
| 4 | 182 | 0.78 | 0.93 | 26 | empty |
| 5 | 108 | 0.74 | 0.95 | 22 | empty |
Interfaces
5 interfaces between chains.
- A–C · 1711 Ų buried · 8 hydrogen bonds · protein-protein
- B–D · 1710 Ų buried · 8 hydrogen bonds · protein-protein
- B–C · 1672 Ų buried · 7 hydrogen bonds · protein-protein
- A–D · 1671 Ų buried · 7 hydrogen bonds · protein-protein
- A–B · 101 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 6ND0 · human BK channel reconstituted into liposomes · the same entry in another collection · chain A against A, 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 A against A, TM-score 0.96
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 6ND0 · PDBe 6ND0 · UniProt Q12791
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