5KHT: PDB entry 5KHT

Crystal structure of the N-terminal fragment of tropomyosin isoform Tpm1.1 at 1.5 A resolution. Determined by X-ray diffraction at 1.5 Å resolution. Released 21 Jun 2017.

Method
X-ray diffraction
Resolution
1.5 Å
Organisms
Homo sapiens, Saccharomyces cerevisiae
Chains
4
Atoms
1,771
Mol. weight
22.24 kDa
Released
21 Jun 2017

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Secondary structure: helices and β-sheets

5KHT contains 4 α-helices and 0 β-strands across 4 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.

Chains A and C: 1 helix, 0 β-strands

ElementResiduesLengthSheet
α-helix1-4343
Chain B: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix2-4342
Chain D: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix4-4340

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Tropomyosin alpha-1 chain,General control protein GCN4A, B, C, Dprotein47Homo sapiens, Saccharomyces cerevisiaeP03069 (AlphaFold model), P09493 (AlphaFold model)
Sequence of entity 1 (A, B, C, D), FASTA
>5KHT_1 Tropomyosin alpha-1 chain,General control protein GCN4 (chains A, B, C, D)
GMDAIKKKMQMLKLDKENALDRAEQAEADNYHLENEVARLKKLVGER

Primary citation

Structural destabilization of tropomyosin induced by the cardiomyopathy-linked mutation R21H. Ly, T., Krieger, I., Tolkatchev, D. et al. Protein Sci (2018) 27:498-508. DOI 10.1002/pro.3341 · PubMed

Other PDB entries of the same protein (UniProt P03069 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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