2M3S: Calmodulin

Calmodulin, i85l, f92e, h107i, l112r, a128t, m144r mutant. Determined by solution NMR. Released 24 Jul 2013.

Method
Solution NMR
Organism
Gallus gallus
Chains
1
Atoms
1,195
Mol. weight
17.27 kDa
Ligands
CA
Released
24 Jul 2013

Explore 2M3S in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2M3S 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-helix9-2012
β-strand3011
α-helix32-409
α-helix48-5811
β-strand6611
α-helix68-7811
α-helix84-9512
β-strand10312
α-helix105-11511
α-helix121-13111
β-strand13912
α-helix141-15010

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
CalmodulinAprotein151Gallus gallusP62149 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2M3S_1 Calmodulin (chains A)
SLMADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDA
DGNGTIDFPEFLTMMARKMKDTDSEEELREAFRVEDKDGNGYISAAELRIVMTNRGEKLT
DEEVDEMIRETDIDGDGQVNYEEFVQRMTAK

Ligands and cofactors

IDNameFormulaCopies
CACalcium ionCa4

Primary citation

A single mutation in a regulatory protein produces evolvable allosterically regulated catalyst of nonnatural reaction. Moroz, O.V., Moroz, Y.S., Wu, Y. et al. Angew Chem Int Ed Engl (2013) 52:6246-6249. DOI 10.1002/anie.201302339 · PubMed

Other PDB entries of the same protein (UniProt P62149 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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