MolNFT v1 · #139876 · protein
Structure of the NAV1.4-BETA1 complex from electric eel
5XSY: “Structure of the NAV1.4-BETA1 complex from electric eel”. Electron microscopy, 2 ligands (NAG, BMA). MolNFT v1 #139876 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5XSY
- Type
- protein
- Length
- 1,312 residues
- Chains
- 2
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P02719, A0A1L3MZ94
- Ligands
- NAG, BMA
Structure
electron microscopy · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 1140 | — | P02719 |
| B | — | protein | 172 | — | A0A1L3MZ94 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 10 copies · chains A, B
- BMA · beta-D-mannopyranose · sugar · 6 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
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 P02719
- Every structure of UniProt A0A1L3MZ94
- Elsewhere: RCSB PDB 5XSY · PDBe 5XSY · UniProt P02719 · UniProt A0A1L3MZ94
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