MolNFT v1 · #80758 · protein
Open structure of the bk channel gating ring
3U6N · High-conductance CA2+-activated K+ channel protein: “Open structure of the bk channel gating ring”. X-ray diffraction, 1 ligand (CA), 20 pockets (best druggability 0.82). MolNFT v1 #80758 on GenesisL1: 3D structure, binding sites…
- PDB
- 3U6N
- Type
- protein
- Length
- 4,680 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- High-conductance CA2+-activated K+ channel protein
- UniProt
- B7ZC96, F1QYL4
- Ligands
- CA
- Pockets
- 20 · best druggability 0.82
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H | High-conductance CA2+-activated K+ channel protein | protein | 585 | 37% helix, 19% strand | B7ZC96, F1QYL4 |
Ligands and binding sites
- CA · Calcium ion · metal · 8 copies · chains A, H, B, G, C, F, D, E
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 1047 | 0.82 | 0.83 | 96 | empty |
| 2 | 885 | 0.81 | 0.83 | 93 | empty |
| 3 | 1183 | 0.80 | 0.82 | 123 | empty |
| 4 | 962 | 0.80 | 0.82 | 110 | empty |
| 5 | 182 | 0.80 | 0.95 | 26 | empty |
Interfaces
16 interfaces between chains.
- B–H · 872 Ų buried · 9 hydrogen bonds · protein-protein
- E–F · 853 Ų buried · 8 hydrogen bonds · protein-protein
- B–G · 847 Ų buried · 9 hydrogen bonds · protein-protein
- C–F · 846 Ų buried · 7 hydrogen bonds · protein-protein
- A–G · 837 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 3U6N · Open Structure of the BK channel Gating Ring · 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 B7ZC96
- Every structure of UniProt F1QYL4
- Elsewhere: RCSB PDB 3U6N · PDBe 3U6N · UniProt B7ZC96 · UniProt F1QYL4
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