Research workbench
Studies of ion transport in K+ channels
Analyse Studies of ion transport in K+ channels in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6DZ1
- Type
- protein
- Length
- 188 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Potassium channel protein
- UniProt
- C2SWC7
- Ligands
- K
- Pockets
- 1 · best druggability 0.53
Structure
x-ray diffraction · 2 distinct chains · 79% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Potassium channel protein | protein | 95 | 77% helix, 0% strand | C2SWC7 |
| B | Potassium channel protein | protein | 93 | 81% helix, 0% strand | C2SWC7 |
Ligands and binding sites
- K · Potassium ion · metal · 10 copies · chains A, B
- MPD · (4S)-2-methyl-2,4-pentanediol · additive · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 259 | 0.53 | 0.75 | 25 | empty |
Interfaces
1 interface between chains.
- A–B · 269 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 6DZ1 · Studies of Ion Transport in K+ Channels · 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 C2SWC7
- Elsewhere: RCSB PDB 6DZ1 · PDBe 6DZ1 · UniProt C2SWC7
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