Research workbench
Structure of human voltage-gated sodium channel NAV1.7 in complex with auxiliary beta subunits, huwentoxin-IV and saxitoxin (Y1755 up)
Analyse Structure of human voltage-gated sodium channel NAV1.7 in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6J8G
- Type
- protein
- Length
- 1,433 residues
- Chains
- 3
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- O60939, Q15858, Q07699
- Ligands
- 9SL, NAG
Structure
electron microscopy · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| C | — | protein | 120 | — | O60939 |
| A | — | protein | 1140 | — | Q15858 |
| B | — | protein | 173 | — | Q07699 |
Ligands and binding sites
- 9SL · [(3aS,4R,10aS)-2,6-diamino-10,10-dihydroxy-3a,4,9,10-tetrahydro-3H,8H-pyrrolo[1,2-c]purin-4-yl]methyl carbamate · ligand · chains A
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 11 copies · chains A, C, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6J8G · Structure of human voltage-gated sodium channel Nav1.7 in complex with auxiliary beta… · the same entry in another collection · chain C against C, TM-score 1.00
- Q15858 · AlphaFold monomer V2.0 prediction for sodium channel protein type 9 subunit alpha (Q15858) · a predicted model of the same protein · chain A against A, TM-score 0.99
- O60939 · AlphaFold monomer V2.0 prediction for sodium channel subunit beta-2 (O60939) · a predicted model of the same protein · chain C against A, TM-score 0.98
- Q07699 · AlphaFold monomer V2.0 prediction for sodium channel subunit beta-1 (Q07699) · a predicted model of the same protein · chain B against A, TM-score 0.92
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 O60939
- Every structure of UniProt Q15858
- Every structure of UniProt Q07699
- Elsewhere: RCSB PDB 6J8G · PDBe 6J8G · UniProt O60939 · UniProt Q15858 · UniProt Q07699
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