3IF7: Calmodulin

Structure of Calmodulin complexed with its first endogenous inhibitor, sphingosylphosphorylcholine. Determined by X-ray diffraction at 1.6 Å resolution. Released 30 Jun 2010.

Method
X-ray diffraction
Resolution
1.6 Å
Organism
Bos taurus
Chains
1
Atoms
1,256
Mol. weight
18.74 kDa
Ligands
CA, SPU
Released
30 Jun 2010

Explore 3IF7 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3IF7 contains 8 α-helices and 4 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: 8 helices, 4 β-strands

ElementResiduesLengthSheet
α-helix6-1914
β-strand26-2721
α-helix29-3810
α-helix45-5511
β-strand63-6421
α-helix65-7410
α-helix82-9211
β-strand99-10022
α-helix102-11110
α-helix118-12811
β-strand136-13722
α-helix138-1458

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
CalmodulinAprotein148Bos taurusP62157 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>3IF7_1 Calmodulin (chains A)
ADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGN
GTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEE
VDEMIREADIDGDGQVNYEEFVQMMTAK

Ligands and cofactors

IDNameFormulaCopies
CACalcium ionCa4
SPU2-{[(R)-{[(2S,3R,4E)-2-amino-3-hydroxyoctadec-4-en-1-yl]oxy}(hydroxy)phosphoryl…C23 H50 N2 O5 P4

Primary citation

Structure and mechanism of calmodulin binding to a signaling sphingolipid reveal new aspects of lipid-protein interactions. Kovacs, E., Harmat, V., Toth, J. et al. FASEB J (2010) 24:3829-3839. DOI 10.1096/fj.10-155614 · 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 3IF7 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.