Research workbench
Structure of K+ selective nak mutant in caesium
Analyse Structure of K+ selective nak mutant in caesium in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4PDL
- Type
- protein
- Length
- 189 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Potassium channel protein
- UniProt
- Q81HW2
- Ligands
- CS, NA
Structure
x-ray diffraction · 2 distinct chains · 77% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Potassium channel protein | protein | 93 | 77% helix, 0% strand | Q81HW2 |
| B | Potassium channel protein | protein | 96 | 77% helix, 0% strand | Q81HW2 |
Ligands and binding sites
- CS · Cesium ion · metal · 5 copies · chains A, B
- NA · Sodium ion · metal · chains A
- MPD · (4S)-2-methyl-2,4-pentanediol · additive · 3 copies · chains A, B
- HEX · Hexane · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 4PDL · Structure of K+ selective NaK mutant in caesium · 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 Q81HW2
- Elsewhere: RCSB PDB 4PDL · PDBe 4PDL · UniProt Q81HW2
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.