Research workbench
The molecular basis of vitamin E retention: structure of human alpha-tocopherol transfer protein
Analyse The molecular basis of vitamin E retention: structure of human alpha-tocopherol… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1OIP
- Type
- protein
- Length
- 251 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha-tocopherol transfer protein
- UniProt
- P49638
- Ligands
- VIV, SO4
- Pockets
- 3 · best druggability 0.87
Structure
x-ray diffraction · 1 distinct chain · 55% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alpha-tocopherol transfer protein | protein | 251 | 55% helix, 11% strand | 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
- SO4 · Sulfate ion · ion · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 341 | 0.87 | 0.95 | 33 | VIV |
| 2 | 80 | 0.41 | 0.79 | 16 | SO4 |
| 3 | 50 | 0.25 | 0.73 | 12 | empty |
Compared structures
- 1OIP · The Molecular Basis of Vitamin E Retention: Structure of Human Alpha-Tocopherol Transfer… · 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 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 P49638
- Elsewhere: RCSB PDB 1OIP · PDBe 1OIP · UniProt P49638
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