1OIP
The Molecular Basis of Vitamin E Retention: Structure of Human Alpha-Tocopherol Transfer Protein
Summary for 1OIP
Entry DOI | 10.2210/pdb1oip/pdb |
Related | 1OIZ 1R5L |
Descriptor | ALPHA-TOCOPHEROL TRANSFER PROTEIN, SULFATE ION, (2R)-2,5,7,8-TETRAMETHYL-2-[(4R,8R)-4,8,12-TRIMETHYLTRIDECYL]CHROMAN-6-OL, ... (4 entities in total) |
Functional Keywords | transport, ataxia, aved, transfer protein, tocopherol, vitamin e transport, disease mutation |
Biological source | HOMO SAPIENS (HUMAN) |
Cellular location | Cytoplasm: P49638 |
Total number of polymer chains | 1 |
Total formula weight | 32414.48 |
Authors | Meier, R.,Tomizaki, T.,Schulze-Briese, C.,Baumann, U.,Stocker, A. (deposition date: 2003-06-24, release date: 2004-01-14, Last modification date: 2024-05-08) |
Primary citation | Meier, R.,Tomizaki, T.,Schulze-Briese, C.,Baumann, U.,Stocker, A. The Molecular Basis of Vitamin E Retention: Structure of Human Alpha-Tocopherol Transfer Protein J.Mol.Biol., 331:725-, 2003 Cited by PubMed: 12899840DOI: 10.1016/S0022-2836(03)00724-1 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.95 Å) |
Structure validation
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