6XXX: Calmodulin-1

1.25 Angstrom crystal structure of Ca/CaM A102V:RyR2 peptide complex. Determined by X-ray diffraction at 1.25 Å resolution. Released 10 Feb 2021.

Method
X-ray diffraction
Resolution
1.25 Å
Organism
Homo sapiens
Chains
2
Atoms
1,621
Mol. weight
19.55 kDa
Ligands
CA
Released
10 Feb 2021

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

Secondary structure: helices and β-sheets

6XXX 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 AAA: 8 helices, 4 β-strands

ElementResiduesLengthSheet
α-helix7-2014
β-strand27-2821
α-helix30-3910
α-helix46-5611
β-strand64-6521
α-helix66-7611
α-helix82-9312
β-strand100-10122
α-helix103-11210
α-helix119-12911
β-strand137-13822
α-helix139-1468
Chain BBB: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix2-1817

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Calmodulin-1AAAprotein149Homo sapiensP0DP23 (AlphaFold model)
Lys-lys-ala-val-trp-his-lys-leu-leu-ser-lys-gln-arg-lys-arg-ala-val-val-ala-cys-pheBBBprotein21Homo sapiens
Sequence of entity 1 (AAA), FASTA
>6XXX_1 Calmodulin-1 (chains AAA)
MADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADG
NGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISVAELRHVMTNLGEKLTDE
EVDEMIREADIDGDGQVNYEEFVQMMTAK
Sequence of entity 2 (BBB), FASTA
>6XXX_2 LYS-LYS-ALA-VAL-TRP-HIS-LYS-LEU-LEU-SER-LYS-GLN-ARG-LYS-ARG-ALA-VAL-VAL-ALA-CYS-PHE (chains BBB)
KKAVWHKLLSKQRKRAVVACF

Ligands and cofactors

IDNameFormulaCopies
CACalcium ionCa4

Primary citation

CPVT-associated calmodulin variants N53I and A102V dysregulate Ca2+ signalling via different mechanisms. Prakash, O., Held, M., McCormick, L.F. et al. J Cell Sci (2022) 135. DOI 10.1242/jcs.258796 · 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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