PDBe 1a2x

X-ray diffraction
2.3Å resolution

COMPLEX OF TROPONIN C WITH A 47 RESIDUE (1-47) FRAGMENT OF TROPONIN I

Released:
Source organism: Oryctolagus cuniculus
Primary publication:
Crystal structure of troponin C in complex with troponin I fragment at 2.3-A resolution.
Proc. Natl. Acad. Sci. U.S.A. 95 4847-52 (1998)
PMID: 9560191

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Troponin C, skeletal muscle Chain: A
Molecule details ›
Chain: A
Length: 159 amino acids
Theoretical weight: 17.98 KDa
Source organism: Oryctolagus cuniculus
Expression system: Escherichia coli
UniProt:
  • Canonical: P02586 (Residues: 2-160; Coverage: 99%)
Gene name: TNNC2
Sequence domains:
Structure domains: EF-hand
Troponin I, fast skeletal muscle Chain: B
Molecule details ›
Chain: B
Length: 47 amino acids
Theoretical weight: 5.55 KDa
Source organism: Oryctolagus cuniculus
Expression system: Escherichia coli
UniProt:
  • Canonical: P02643 (Residues: 2-48; Coverage: 26%)
Gene name: TNNI2

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM14
Spacegroup: P3221
Unit cell:
a: 46.9Å b: 46.9Å c: 152.3Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.222 0.222 0.325
Expression system: Escherichia coli