Research workbench
Structure of the intracellular gating ring from the human high- conductance CA2+ gated K+ channel (bk channel)
Analyse Structure of the intracellular gating ring from the human high- conductance… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3NAF
- Type
- protein
- Length
- 648 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Calcium-activated potassium channel subunit alpha-1, calcium-activated potassium channel…
- UniProt
- Q12791
- Pockets
- 10 · best druggability 0.74
Structure
x-ray diffraction · 1 distinct chain · 32% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Calcium-activated potassium channel subunit alpha-1, calcium-activated potassium channel subunit alpha-1,CALCIUM-activated potassium channel subunit alpha-1 | protein | 648 | 32% helix, 17% strand | Q12791 |
Pockets
10 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 94 | 0.74 | 0.96 | 24 | empty |
| 2 | 167 | 0.74 | 0.91 | 37 | empty |
| 3 | 298 | 0.62 | 0.80 | 38 | empty |
| 4 | 181 | 0.58 | 0.81 | 19 | empty |
| 5 | 205 | 0.56 | 0.79 | 32 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 3NAF · Structure of the Intracellular Gating Ring from the Human High-conductance Ca2+ gated K+… · 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 0.95
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 3NAF · PDBe 3NAF · UniProt Q12791
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