6U3B: Calmodulin-1

1.7 Angstrom crystal structure of the Q135P Ca-CaM:CaV1.2 IQ domain complex. Determined by X-ray diffraction at 1.7 Å resolution. Released 19 Feb 2020.

Method
X-ray diffraction
Resolution
1.7 Å
Organism
Homo sapiens
Chains
2
Atoms
1,614
Mol. weight
21.21 kDa
Ligands
CA
Released
19 Feb 2020

Explore 6U3B in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6U3B contains 10 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-helix45-5511
β-strand63-6421
α-helix65-7612
α-helix82-9211
β-strand99-10022
α-helix102-11110
α-helix118-12811
β-strand136-13722
α-helix138-1458
Chain B: 2 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix1610-16134
α-helix1614-163623

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Calmodulin-1Aprotein148Homo sapiensP0DP23 (AlphaFold model)
Voltage-dependent L-type calcium channel subunit alpha-1CBprotein37Homo sapiensQ13936 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>6U3B_1 Calmodulin-1 (chains A)
ADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGN
GTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEE
VDEMIREADIDGDGPVNYEEFVQMMTAK
Sequence of entity 2 (B), FASTA
>6U3B_2 Voltage-dependent L-type calcium channel subunit alpha-1C (chains B)
SNADEVTVGKFYATFLIQEYFRKFKKRKEQGLVGKPS

Ligands and cofactors

IDNameFormulaCopies
CACalcium ionCa5

Primary citation

Arrhythmia mutations in calmodulin can disrupt cooperativity of Ca2+binding and cause misfolding. Wang, K., Brohus, M., Holt, C. et al. J Physiol (2020) 598:1169-1186. DOI 10.1113/JP279307 · PubMed

Other PDB entries of the same protein (UniProt P0DP23 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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