1AK8: Calmodulin

NMR solution structure of cerium-loaded calmodulin amino-terminal domain (CE2-TR1C), 23 structures. Determined by solution NMR. Released 17 Sept 1997.

Method
Solution NMR
Organism
Bos taurus
Chains
1
Atoms
591
Mol. weight
8.73 kDa
Ligands
CE
Released
17 Sept 1997

Explore 1AK8 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1AK8 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-helix6-1914
β-strand2711
α-helix30-3910
α-helix45-528
β-strand6311
α-helix65-7410

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
CalmodulinAprotein76Bos taurusP62157 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1AK8_1 CALMODULIN (chains A)
MADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADG
NGTIDFPEFLTMMARK

Ligands and cofactors

IDNameFormulaCopies
CECerium (III) ionCe2

Primary citation

Solution structure of the paramagnetic complex of the N-terminal domain of calmodulin with two Ce3+ ions by 1H NMR. Bentrop, D., Bertini, I., Cremonini, M.A. et al. Biochemistry (1997) 36:11605-11618. DOI 10.1021/bi971022+ · 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 1AK8 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.