MolNFT v1 · #49617 · protein
An anisotropic model for potassium channel kcsa
2QTO · Voltage-gated potassium channel: “An anisotropic model for potassium channel kcsa”. X-ray diffraction, 1 ligand (K), 7 pockets (best druggability 0.86). MolNFT v1 #49617 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2QTO
- Type
- protein
- Length
- 388 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Voltage-gated potassium channel
- UniProt
- P0A334
- Ligands
- K
- Pockets
- 7 · best druggability 0.86
Structure
x-ray diffraction · 1 distinct chain · 71% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Voltage-gated potassium channel | protein | 97 | 71% helix, 0% strand | P0A334 |
Ligands and binding sites
- K · Potassium ion · metal · 3 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 418 | 0.86 | 0.94 | 32 | empty |
| 2 | 146 | 0.44 | 0.76 | 30 | empty |
| 3 | 141 | 0.43 | 0.75 | 25 | empty |
| 4 | 129 | 0.42 | 0.75 | 26 | empty |
| 5 | 101 | 0.37 | 0.75 | 21 | empty |
Interfaces
6 interfaces between chains.
- C–D · 993 Ų buried · 5 hydrogen bonds · protein-protein
- A–D · 992 Ų buried · 5 hydrogen bonds · protein-protein
- A–B · 983 Ų buried · 5 hydrogen bonds · protein-protein
- B–C · 973 Ų buried · 5 hydrogen bonds · protein-protein
- A–C · 48 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 2QTO · An anisotropic model for potassium channel KcsA · 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 P0A334
- Elsewhere: RCSB PDB 2QTO · PDBe 2QTO · UniProt P0A334
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