1FW4: Calmodulin

Crystal structure of E. Coli fragment TR2C from calmodulin to 1.7 a resolution. Determined by X-ray diffraction at 1.7 Å resolution. Released 2 May 2001.

Method
X-ray diffraction
Resolution
1.7 Å
Organism
Bos taurus
Chains
1
Atoms
575
Mol. weight
8.24 kDa
Ligands
CA
Released
2 May 2001

Explore 1FW4 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1FW4 contains 4 α-helices and 2 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 4 helices, 2 β-strands

ElementResiduesLengthSheet
α-helix83-9210
β-strand99-10021
α-helix102-11110
α-helix118-1269
β-strand136-13721
α-helix138-1447

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
CalmodulinAprotein71Bos taurusP62157 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1FW4_1 CALMODULIN (chains A)
DTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEEVDEMIREADIDGDGQVN
YEEFVQMMTAK

Ligands and cofactors

IDNameFormulaCopies
CACalcium ionCa2

Primary citation

Structure of Escherichia coli fragment TR2C from calmodulin to 1.7 A resolution. Olsson, L.L., Sjolin, L. Acta Crystallogr D Biol Crystallogr (2001) 57:664-669. DOI 10.1107/S090744490100347X · PubMed

Other PDB entries of the same protein (UniProt P62157 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

About this viewer

MolViewer shows 1FW4 directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.