1CDM: Peptide calmodulin-dependent protein kinase II

Modulation of calmodulin plasticity in molecular recognition on the basis of X-ray structures. Determined by X-ray diffraction at 2.0 Å resolution. Released 31 Aug 1994.

Method
X-ray diffraction
Resolution
2.0 Å
Organism
Bos taurus
Chains
2
Atoms
1,236
Mol. weight
19.32 kDa
Ligands
CA
Released
31 Aug 1994

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

Secondary structure: helices and β-sheets

1CDM contains 9 α-helices and 4 β-strands across 2 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-helix45-539
β-strand63-6421
α-helix65-728
α-helix85-928
β-strand99-10022
α-helix102-11110
α-helix118-12811
β-strand136-13722
α-helix138-1458
Chain B: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix295-30915

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Peptide calmodulin-dependent protein kinase IIAprotein144Bos taurusP62157 (AlphaFold model)
CalmodulinBprotein25P11275 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1CDM_1 PEPTIDE CALMODULIN-DEPENDENT PROTEIN KINASE II (chains A)
LTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTI
DFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEEVDE
MIREADIDGDGQVNYEEFVQMMTA
Sequence of entity 2 (B), FASTA
>1CDM_2 CALMODULIN (chains B)
LKKFNARRKLKGAILTTMLATRNFS

Ligands and cofactors

IDNameFormulaCopies
CACalcium ionCa4

Primary citation

Modulation of calmodulin plasticity in molecular recognition on the basis of x-ray structures. Meador, W.E., Means, A.R., Quiocho, F.A. Science (1993) 262:1718-1721. PubMed

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

Browse structure collections

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