Research workbench
Mechanism of activation gating in the full-length kcsa K+ channel
Analyse Mechanism of activation gating in the full-length kcsa K+ channel in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3PJS
- Type
- protein
- Length
- 1,424 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fab light chain; Fab heavy chain; Voltage-gated potassium channel
- UniProt
- P0A334
- Pockets
- 16 · best druggability 0.78
Structure
x-ray diffraction · 3 distinct chains · 12% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Fab light chain | protein | 215 | 2% helix, 44% strand | — |
| B, D | Fab heavy chain | protein | 219 | 4% helix, 46% strand | — |
| K, L, M, N | Voltage-gated potassium channel | protein | 139 | 41% helix, 0% strand | P0A334 |
Pockets
16 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1011 | 0.78 | 0.80 | 107 | empty |
| 2 | 945 | 0.72 | 0.76 | 58 | empty |
| 3 | 176 | 0.58 | 0.81 | 26 | empty |
| 4 | 147 | 0.51 | 0.78 | 24 | empty |
| 5 | 269 | 0.50 | 0.74 | 41 | empty |
Interfaces
14 interfaces between chains.
- C–D · 1858 Ų buried · 7 hydrogen bonds · protein-protein
- A–B · 1824 Ų buried · 8 hydrogen bonds · protein-protein
- K–L · 1531 Ų buried · 27 hydrogen bonds · protein-protein
- M–N · 1389 Ų buried · 29 hydrogen bonds · protein-protein
- L–M · 1194 Ų buried · 23 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 disulfide (disulfide).
Compared structures
- 3PJS · Mechanism of Activation Gating in the Full-Length KcsA K+ Channel · 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 P0A334
- Elsewhere: RCSB PDB 3PJS · PDBe 3PJS · UniProt P0A334
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