Research workbench
K+ complex of the nak channel
Analyse K+ complex of the nak channel in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2AHZ
- Type
- protein
- Length
- 208 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Potassium channel protein
- Ligands
- K, CA
- Pockets
- 2 · best druggability 0.74
Structure
x-ray diffraction · 2 distinct chains · 77% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Potassium channel protein | protein | 105 | 77% helix, 0% strand | — |
| B | Potassium channel protein | protein | 103 | 78% helix, 0% strand | — |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 667 | 0.74 | 0.79 | 60 | empty |
| 2 | 53 | 0.35 | 0.78 | 11 | empty |
Interfaces
1 interface between chains.
- A–B · 1247 Ų buried · 13 hydrogen bonds · protein-protein
Compared structures
- 2AHZ · K+ complex of the NaK Channel · 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 2AHZ · PDBe 2AHZ
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