MolNFT v1 · #82492 · protein
The crystal structure of nak-navsulp chimera channel
3VOU · Ion transport 2 domain protein, voltage-gated sodium channel: “The crystal structure of nak-navsulp chimera channel”. X-ray diffraction, 2 ligands (NA, CO), 2 pockets (best druggability 0.70). MolNFT v1 #82492 on GenesisL1: 3D…
- PDB
- 3VOU
- Type
- protein
- Length
- 275 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ion transport 2 domain protein, voltage-gated sodium channel
- UniProt
- A9VEV6, A3SUL8
- Ligands
- NA, CO
- Pockets
- 2 · best druggability 0.70
Structure
x-ray diffraction · 2 distinct chains · 78% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ion transport 2 domain protein, voltage-gated sodium channel | protein | 139 | 81% helix, 0% strand | A9VEV6, A3SUL8 |
| B | Ion transport 2 domain protein, voltage-gated sodium channel | protein | 136 | 76% helix, 0% strand | A9VEV6, A3SUL8 |
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 | 630 | 0.70 | 0.78 | 58 | empty |
| 2 | 55 | 0.40 | 0.80 | 10 | empty |
Interfaces
1 interface between chains.
- A–B · 1851 Ų buried · 14 hydrogen bonds · protein-protein
Compared structures
- 3VOU · The crystal structure of NaK-NavSulP chimera 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
- Every structure of UniProt A9VEV6
- Every structure of UniProt A3SUL8
- Elsewhere: RCSB PDB 3VOU · PDBe 3VOU · UniProt A9VEV6 · UniProt A3SUL8
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