MolNFT v1 · #127364 · protein
Self-assembled alpha-tocopherol transfer protein nanoparticles promote vitamin E delivery across an endothelial barrier
5MUG: “Self-assembled alpha-tocopherol transfer protein nanoparticles promote vitamin E delivery across an…”. X-ray diffraction, 4 ligands (VIV, ETA, CL). MolNFT v1 #127364 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5MUG
- Type
- protein
- Length
- 231 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P49638
- Ligands
- VIV, ETA, CL, SO4
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 231 | — | P49638 |
Ligands and binding sites
- VIV · (2R)-2,5,7,8-tetramethyl-2-[(4R,8R)-4,8,12-trimethyltridecyl]chroman-6-ol · ligand · chains A
- ETA · Ethanolamine · ligand · chains A
- CL · Chloride ion · ion · 2 copies · chains A
- SO4 · Sulfate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5MUG · Self-assembled alpha-Tocopherol Transfer Protein Nanoparticles Promote Vitamin E Delivery… · the same entry in another collection · chain A against A, TM-score 1.00
- P49638 · AlphaFold monomer V2.0 prediction for alpha-tocopherol transfer protein (P49638) · a predicted model of the same protein · chain A against A, TM-score 0.97
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 P49638
- Elsewhere: RCSB PDB 5MUG · PDBe 5MUG · UniProt P49638
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