› 5kht

X-ray diffraction
1.5Å resolution

Crystal structure of the N-terminal fragment of tropomyosin isoform Tpm1.1 at 1.5 A resolution

Released:
DOI: 10.2210/pdb5kht/pdb
PDB entry 5kht coloured by chain, front view.
PDB entry 5kht coloured by chain, side view.
PDB entry 5kht coloured by chain, top view.
Source organisms:
Primary publication:
Structural destabilization of tropomyosin induced by the cardiomyopathy-linked mutation R21H.
Ly T, Krieger I, Tolkatchev D, Krone C, Moural T, Samatey FA, Kang C, Kostyukova AS
Protein Sci 27 498-508 (2018)
PMID: 29105867

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-136507 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
General control transcription factor GCN4; Tropomyosin alpha-1 chain Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 47 amino acids
Theoretical weight: 5.45 KDa
Source organisms: Expression system: Escherichia coli
UniProt:
  • Canonical: P09493 (Residues: 1-28; Coverage: 10%)
  • Canonical: P03069 (Residues: 264-281; Coverage: 6%)
Gene names: AAS101, AAS3, ARG9, C15orf13, GCN4, TMSA, TPM1, YEL009C
Sequence domains: Tropomyosin
Structure domains: Vasodilator-stimulated phosphoprotein

Ligands and Environments

1 bound ligand:
Ligand PEG 4 x PEG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X6A
Spacegroup: P1
Unit cell:
a: 35.97Å b: 36.47Å c: 36.71Å
α: 65.21° β: 74.71° γ: 78.98°
R-values:
R R work R free
0.209 0.206 0.249
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Thin filament dysfunctions caused by mutations in tropomyosin Tpm3.12 and Tpm1.1.
Moraczewska J. (2020)
1 more

4 mentions without citation

Lack of evidence of significant homology of SARS-CoV-2 spike sequences to myocarditis-associated antigens.
Marrama et al. (2022)
3 more