Research workbench
Potassium channel from magnetospirillum magnetotacticum
Analyse Potassium channel from magnetospirillum magnetotacticum in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2WLN
- Type
- protein
- Length
- 2,264 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Potassium channel
- Ligands
- K
- Pockets
- 20 · best druggability 0.83
Structure
x-ray diffraction · 1 distinct chain · 31% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H | Potassium channel | protein | 283 | 31% helix, 33% strand | — |
Ligands and binding sites
- K · Potassium ion · metal · 6 copies · chains A, B, C, D, E, F, G, H
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 16 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1101 | 0.83 | 0.84 | 95 | empty |
| 2 | 980 | 0.83 | 0.84 | 99 | empty |
| 3 | 960 | 0.83 | 0.84 | 96 | empty |
| 4 | 675 | 0.80 | 0.84 | 72 | empty |
| 5 | 532 | 0.75 | 0.83 | 43 | empty |
Interfaces
15 interfaces between chains.
- E–F · 2369 Ų buried · 28 hydrogen bonds · protein-protein
- G–H · 2336 Ų buried · 26 hydrogen bonds · protein-protein
- B–C · 2313 Ų buried · 24 hydrogen bonds · protein-protein
- A–D · 2300 Ų buried · 25 hydrogen bonds · protein-protein
- C–D · 2285 Ų buried · 21 hydrogen bonds · protein-protein
Compared structures
- 2WLN · Potassium channel from magnetospirillum magnetotacticum · 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
- Elsewhere: RCSB PDB 2WLN · PDBe 2WLN
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