1MXE: Calmodulin

Structure of the Complex of Calmodulin with the Target Sequence of CaMKI. Determined by X-ray diffraction at 1.7 Å resolution. Released 4 Dec 2002.

Method
X-ray diffraction
Resolution
1.7 Å
Organism
Drosophila melanogaster
Chains
4
Atoms
2,922
Mol. weight
39.7 kDa
Ligands
CA
Released
4 Dec 2002

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

Secondary structure: helices and β-sheets

1MXE contains 18 α-helices and 8 β-strands across 4 chains. 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-helix65-7814
α-helix81-9212
β-strand99-10022
α-helix102-11110
α-helix118-12811
β-strand136-13722
α-helix138-1469
Chain B: 8 helices, 4 β-strands
ElementResiduesLengthSheet
α-helix6-1914
β-strand26-2723
α-helix29-3810
α-helix45-5511
β-strand63-6423
α-helix65-7713
α-helix81-9212
β-strand10014
α-helix102-11110
α-helix118-12811
β-strand13614
α-helix138-1469
Chains E and F: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix298-31720

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
CalmodulinA, Bprotein148Drosophila melanogasterP62152 (AlphaFold model)
Target Sequence of rat Calmodulin-Dependent Protein Kinase IE, Fprotein25Q63450 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>1MXE_1 Calmodulin (chains A, B)
ADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGN
GTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGFISAAELRHVMTNLGEKLTDEE
VDEMIREADIDGDGQVNYEEFVTMMTSK
Sequence of entity 2 (E, F), FASTA
>1MXE_2 Target Sequence of rat Calmodulin-Dependent Protein Kinase I (chains E, F)
IKKNFAKSKWKQAFNATAVVRHMRK

Ligands and cofactors

IDNameFormulaCopies
CACalcium ionCa8

Primary citation

Structure of the Complex of Calmodulin with the Target Sequence of Calmodulin-Dependent Protein Kinase I: Studies of the Kinase Activation Mechanism. Clapperton, J.A., Martin, S.R., Smerdon, S.J. et al. Biochemistry (2002) 41:14669-14679. DOI 10.1021/bi026660t · PubMed

Other PDB entries of the same protein (UniProt P62152 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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