2KDU: Calmodulin

Structural basis of the Munc13-1/Ca2+-Calmodulin interaction: A novel 1-26 calmodulin binding motif with a bipartite binding mode. Determined by solution NMR. Released 15 Dec 2009.

Method
Solution NMR
Organism
Xenopus laevis
Chains
2
Atoms
1,463
Mol. weight
21.06 kDa
Ligands
CA
Released
15 Dec 2009

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

Secondary structure: helices and β-sheets

2KDU contains 12 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: 10 helices, 4 β-strands

ElementResiduesLengthSheet
α-helix3-53
α-helix6-1914
β-strand26-2831
α-helix29-3810
α-helix45-5511
α-helix57-593
β-strand62-6431
α-helix65-7410
α-helix84-929
β-strand10012
α-helix102-11110
α-helix118-12811
β-strand13612
α-helix138-1458
Chain B: 2 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix459-47820
α-helix487-4904

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
CalmodulinAprotein148Xenopus laevisP0DP33 (AlphaFold model)
Protein unc-13 homolog ABprotein36Q62768 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2KDU_1 Calmodulin (chains A)
ADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGN
GTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEE
VDEMIREADIDGDGQVNYEEFVQMMTAK
Sequence of entity 2 (B), FASTA
>2KDU_2 Protein unc-13 homolog A (chains B)
GSRAKANWLRAFNKVRMQLQEARGEGEMSKSLWFKG

Ligands and cofactors

IDNameFormulaCopies
CACalcium ionCa4

Primary citation

Modular architecture of Munc13/calmodulin complexes: dual regulation by Ca2+ and possible function in short-term synaptic plasticity. Rodriguez-Castaneda, F., Maestre-Martinez, M., Coudevylle, N. et al. EMBO J (2010) 29:680-691. DOI 10.1038/emboj.2009.373 · PubMed

Other PDB entries of the same protein (UniProt P0DP33 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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