Transthyretin THR119MET protein stabilisation. Determined by X-ray diffraction at 1.1 Å resolution. Released 29 Jun 2001.
Explore 1F86 in 3D Show helices and sheets RCSB PDB PDBe
1F86 contains 2 α-helices and 22 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 12-18 | 7 | 1 |
| β-strand | 23-24 | 2 | 1 |
| β-strand | 29-35 | 7 | 2 |
| β-strand | 41-48 | 8 | 2 |
| β-strand | 54-55 | 2 | 1 |
| β-strand | 67-73 | 7 | 2 |
| α-helix | 75-81 | 7 | |
| β-strand | 88-90 | 3 | 3 |
| β-strand | 91-97 | 7 | 2 |
| β-strand | 99 | 1 | 4 |
| β-strand | 101 | 1 | 4 |
| β-strand | 104-112 | 9 | 1 |
| β-strand | 115-123 | 9 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 12-18 | 7 | 1 |
| β-strand | 23-24 | 2 | 1 |
| β-strand | 29-35 | 7 | 3 |
| β-strand | 41-48 | 8 | 3 |
| β-strand | 54-55 | 2 | 1 |
| β-strand | 67-73 | 7 | 3 |
| α-helix | 75-81 | 7 | |
| β-strand | 88-90 | 3 | 2 |
| β-strand | 91-97 | 7 | 3 |
| β-strand | 104-111 | 8 | 1 |
| β-strand | 115-123 | 9 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Transthyretin THR119MET variant | A, B | protein | 115 | Homo sapiens | P02766 (AlphaFold model) |
>1F86_1 TRANSTHYRETIN THR119MET VARIANT (chains A, B) CPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIY KVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTMAVVTN
| ID | Name | Formula | Copies |
|---|---|---|---|
| T44 | 3,5,3',5'-tetraiodo-L-thyronine | C15 H11 I4 N O4 | 2 |
Transthyretin stability as a key factor in amyloidogenesis: X-ray analysis at atomic resolution. Sebastiao, M.P., Lamzin, V., Saraiva, M.J. et al. J Mol Biol (2001) 306:733-744. DOI 10.1006/jmbi.2000.4415 · PubMed
Other PDB entries of the same protein (UniProt P02766 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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