Research workbench
Human K2P4.1 (traaak) potassium channel, W262S mutant
Analyse Human K2P4.1 (traaak) potassium channel, W262S mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4RUF
- Type
- protein
- Length
- 508 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Potassium channel subfamily K member 4
- UniProt
- Q9NYG8
- Ligands
- K
- Pockets
- 8 · best druggability 0.78
Structure
x-ray diffraction · 2 distinct chains · 72% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Potassium channel subfamily K member 4 | protein | 257 | 70% helix, 0% strand | Q9NYG8 |
| B | Potassium channel subfamily K member 4 | protein | 251 | 74% helix, 0% strand | Q9NYG8 |
Ligands and binding sites
- K · Potassium ion · metal · 6 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 967 | 0.78 | 0.81 | 110 | K |
| 2 | 993 | 0.74 | 0.77 | 78 | K |
| 3 | 136 | 0.67 | 0.88 | 20 | empty |
| 4 | 116 | 0.62 | 0.86 | 20 | empty |
| 5 | 206 | 0.54 | 0.78 | 22 | empty |
Interfaces
1 interface between chains.
- A–B · 5186 Ų buried · 46 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 4RUF · Human K2P4.1 (TRAAAK) potassium channel, W262S mutant · the same entry in another collection · chain A against A, TM-score 1.00
- Q9NYG8 · AlphaFold monomer V2.0 prediction for potassium channel subfamily K member 4 (Q9NYG8) · a predicted model of the same protein · chain B against A, TM-score 0.93
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 Q9NYG8
- Elsewhere: RCSB PDB 4RUF · PDBe 4RUF · UniProt Q9NYG8
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