› 1avs

X-ray diffraction
1.75Å resolution

X-RAY CRYSTALLOGRAPHIC STUDY OF CALCIUM-SATURATED N-TERMINAL DOMAIN OF TROPONIN C

Released:
DOI: 10.2210/pdb1avs/pdb
PDB entry 1avs coloured by chain, front view.
PDB entry 1avs coloured by chain, side view.
PDB entry 1avs coloured by chain, top view.
Source organism: Gallus gallus
Primary publication:
Structural details of a calcium-induced molecular switch: X-ray crystallographic analysis of the calcium-saturated N-terminal domain of troponin C at 1.75 A resolution.
Strynadka NC, Cherney M, Sielecki AR, Li MX, Smillie LB, James MN
J Mol Biol 273 238-55 (1997)
PMID: 9367759

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-135940 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Troponin C, skeletal muscle Chains: A, B
Molecule details ›
Chains: A, B
Length: 90 amino acids
Theoretical weight: 9.98 KDa
Source organism: Gallus gallus
Expression system: Escherichia coli
UniProt:
  • Canonical: P02588 (Residues: 2-91; Coverage: 55%)
Gene name: TNNC2
Sequence domains: EF-hand domain pair
Structure domains: EF-hand

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X11
Spacegroup: P21
Unit cell:
a: 32.12Å b: 81.58Å c: 39.86Å
α: 90° β: 112.67° γ: 90°
R-values:
R R work R free
0.22 0.214 0.25
Expression system: Escherichia coli

Quick links

Citations

13 review citations

Regulation of contraction in striated muscle.
Gordon et al. (2000)
12 more

7 mentions without citation

Structure and function of cardiac troponin C (TNNC1): Implications for heart failure, cardiomyopathies, and troponin modulating drugs.
Li et al. (2015)
6 more