MolNFT v1 · #190682 · protein
Human NAV1.7 mutant class-I
7XVE: “Human NAV1.7 mutant class-I”. Electron microscopy, 6 ligands (LPE, PCW, CLR). MolNFT v1 #190682 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7XVE
- Type
- protein
- Length
- 1,570 residues
- Chains
- 3
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q15858, Q07699, O60939
- Ligands
- LPE, PCW, CLR, Y01, 1PW, NAG
Structure
electron microscopy · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 1277 | — | Q15858 |
| B | — | protein | 173 | — | Q07699 |
| C | — | protein | 120 | — | O60939 |
Ligands and binding sites
- LPE · 1-O-octadecyl-sn-glycero-3-phosphocholine · ligand · 18 copies · chains A, B
- PCW · 1,2-dioleoyl-sn-glycero-3-phosphocholine · ligand · 6 copies · chains A
- CLR · Cholesterol · ligand · 4 copies · chains A
- Y01 · Cholesterol hemisuccinate · ligand · chains A
- 1PW · (2S,3R,4E)-2-(acetylamino)-3-hydroxyoctadec-4-en-1-yl dihydrogen phosphate · ligand · chains A
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 11 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7XVE · Human Nav1.7 mutant class-I · the same entry in another collection · chain B against B, TM-score 1.00
- 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
- 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 0.93
- 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 0.93
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 Q15858
- Every structure of UniProt Q07699
- Every structure of UniProt O60939
- Elsewhere: RCSB PDB 7XVE · PDBe 7XVE · UniProt Q15858 · UniProt Q07699 · UniProt O60939
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