1TTA
THE X-RAY CRYSTAL STRUCTURE REFINEMENTS OF NORMAL HUMAN TRANSTHYRETIN AND THE AMYLOIDOGENIC VAL30MET VARIANT TO 1.7 ANGSTROMS RESOLUTION
Summary for 1TTA
Entry DOI | 10.2210/pdb1tta/pdb |
Descriptor | TRANSTHYRETIN (2 entities in total) |
Functional Keywords | transport(thyroxine) |
Biological source | Homo sapiens (human) |
Cellular location | Secreted: P02766 |
Total number of polymer chains | 2 |
Total formula weight | 27554.72 |
Authors | Hamilton, J.A.,Steinrauf, L.K.,Braden, B.C. (deposition date: 1992-11-02, release date: 1993-10-31, Last modification date: 2024-02-14) |
Primary citation | Hamilton, J.A.,Steinrauf, L.K.,Braden, B.C.,Liepnieks, J.,Benson, M.D.,Holmgren, G.,Sandgren, O.,Steen, L. The x-ray crystal structure refinements of normal human transthyretin and the amyloidogenic Val-30-->Met variant to 1.7-A resolution. J.Biol.Chem., 268:2416-2424, 1993 Cited by PubMed: 8428915PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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