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
- 1OIZ
- Type
- protein
- Length
- 529 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha-tocopherol transfer protein
- UniProt
- P49638
- Ligands
- TRT
- Pockets
- 4 · best druggability 0.84
Structure
x-ray diffraction · 2 distinct chains · 55% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alpha-tocopherol transfer protein | protein | 265 | 55% helix, 10% strand | P49638 |
| B | Alpha-tocopherol transfer protein | protein | 264 | 55% helix, 10% strand | P49638 |
Ligands and binding sites
- TRT · Fragment of triton X-100 · ligand · 6 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 717 | 0.84 | 0.87 | 43 | TRT |
| 2 | 702 | 0.84 | 0.87 | 43 | TRT |
| 3 | 356 | 0.55 | 0.74 | 44 | empty |
| 4 | 56 | 0.33 | 0.78 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 678 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 1OIZ · 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 B against A, TM-score 0.96
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 1OIZ · PDBe 1OIZ · UniProt P49638
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