1F86: Transthyretin THR119MET protein stabilisation

Transthyretin THR119MET protein stabilisation. Determined by X-ray diffraction at 1.1 Å resolution. Released 29 Jun 2001.

Method
X-ray diffraction
Resolution
1.1 Å
Organism
Homo sapiens
Chains
2
Atoms
2,182
Mol. weight
26.83 kDa
Ligands
T44
Released
29 Jun 2001

Explore 1F86 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 1 helix, 12 β-strands

ElementResiduesLengthSheet
β-strand12-1871
β-strand23-2421
β-strand29-3572
β-strand41-4882
β-strand54-5521
β-strand67-7372
α-helix75-817
β-strand88-9033
β-strand91-9772
β-strand9914
β-strand10114
β-strand104-11291
β-strand115-12391
Chain B: 1 helix, 10 β-strands
ElementResiduesLengthSheet
β-strand12-1871
β-strand23-2421
β-strand29-3573
β-strand41-4883
β-strand54-5521
β-strand67-7373
α-helix75-817
β-strand88-9032
β-strand91-9773
β-strand104-11181
β-strand115-12391

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Transthyretin THR119MET variantA, Bprotein115Homo sapiensP02766 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>1F86_1 TRANSTHYRETIN THR119MET VARIANT (chains A, B)
CPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIY
KVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTMAVVTN

Ligands and cofactors

IDNameFormulaCopies
T443,5,3',5'-tetraiodo-L-thyronineC15 H11 I4 N O42

Primary citation

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:

Browse structure collections

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