› 6otn

X-ray diffraction
2.4Å resolution

Crystal Structure of an N-terminal Fragment of Cancer Associated Tropomyosin 3.1 (Tpm3.1)

Released:
DOI: 10.2210/pdb6otn/pdb
PDB entry 6otn coloured by chain, front view.
PDB entry 6otn coloured by chain, side view.
PDB entry 6otn coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Molecular integration of the anti-tropomyosin compound ATM-3507 into the coiled coil overlap region of the cancer-associated Tpm3.1.
Janco M, Rynkiewicz MJ, Li L, Hook J, Eiffe E, Ghosh A, Böcking T, Lehman WJ, Hardeman EC, Gunning PW
Sci Rep 9 11262 (2019)
PMID: 31375704

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139207 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tropomyosin alpha-3 chain Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 81 amino acids
Theoretical weight: 9.29 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P06753 (Residues: 44-117; Coverage: 26%)
Gene name: TPM3
Sequence domains: Tropomyosin

Ligands and Environments

1 bound ligand:
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS-II BEAMLINE 17-ID-1
Spacegroup: P43212
Unit cell:
a: 97.201Å b: 97.201Å c: 93.1Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.238 0.235 0.266
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Research Advances in the Role of the Tropomyosin Family in Cancer.
Meng et al. (2023)
7 other articles

2 mentions without citation

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