PDBe 1ytz

X-ray diffraction
3Å resolution

Crystal structure of skeletal muscle troponin in the Ca2+-activated state

Released:
Source organism: Gallus gallus
Primary publication:
Ca(2+)-regulated structural changes in troponin.
Proc. Natl. Acad. Sci. U.S.A. 102 5038-43 (2005)
PMID: 15784741

Function and Biology Details

Structure analysis Details

Assemblies composition:
hetero trimer (preferred)
hetero hexamer
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Troponin C, skeletal muscle Chain: C
Molecule details ›
Chain: C
Length: 162 amino acids
Theoretical weight: 18.26 KDa
Source organism: Gallus gallus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P02588 (Residues: 2-163; Coverage: 99%)
Gene name: TNNC2
Sequence domains:
Structure domains: EF-hand
Troponin I, fast skeletal muscle Chain: I
Molecule details ›
Chain: I
Length: 182 amino acids
Theoretical weight: 21.12 KDa
Source organism: Gallus gallus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P68246 (Residues: 2-183; Coverage: 100%)
Gene name: TNNI2
Sequence domains: Troponin
Structure domains: Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Troponin T, fast skeletal muscle isoforms Chain: T
Molecule details ›
Chain: T
Length: 107 amino acids
Theoretical weight: 12.69 KDa
Source organism: Gallus gallus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P12620 (Residues: 157-263; Coverage: 41%)
Gene name: TNNT3
Structure domains: Single alpha-helices involved in coiled-coils or other helix-helix interfaces

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.3.1
Spacegroup: P43212
Unit cell:
a: 138.608Å b: 138.608Å c: 83.676Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.289 0.289 0.338
Expression system: Escherichia coli BL21(DE3)