Research workbench
NaK S-ELM mutant with Na+ and K+
Analyse NaK S-ELM mutant with Na+ and K+ in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7OQ1
- Type
- protein
- Length
- 187 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.85
- Source
- Bacillus cereus (strain ATCC 14579 / DSM 31 / JCM 2152 / NBRC 15305 / NCIMB…
- Molecule
- Potassium channel protein
- UniProt
- Q81HW2
- Ligands
- K, NA, CL
- Pockets
- 1 · best druggability 0.30
Structure
x-ray diffraction · resolution 1.85 · 2 distinct chains · 77% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Potassium channel protein | protein | 94 | 76% helix, 0% strand | Q81HW2 |
| B | Potassium channel protein | protein | 93 | 78% helix, 0% strand | Q81HW2 |
Ligands and binding sites
- K · Potassium ion · metal · 3 copies · chains A, B
- NA · Sodium ion · metal · 2 copies · chains A, B
- CL · Chloride ion · ion · chains A
- ACT · Acetate ion · additive · 12 copies · chains A, B
- MPD · (4S)-2-methyl-2,4-pentanediol · additive · 7 copies · chains A, B
- MRD · (4R)-2-methylpentane-2,4-diol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 71 | 0.30 | 0.73 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 1117 Ų buried · 10 hydrogen bonds · protein-protein
Compared structures
- 7OQ1 · Nak S-elm mutant with na+ and K+ · 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 7OQ1 · PDBe 7OQ1 · UniProt Q81HW2
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