6BUT: Full-length apo mammalian calmodulin

Solution structure of full-length apo mammalian calmodulin bound to the IQ motif of the human voltage-gated sodium channel NaV1.2. Determined by solution NMR. Released 19 Jun 2019.

Method
Solution NMR
Organism
Homo sapiens
Chains
2
Atoms
1,425
Mol. weight
20.4 kDa
Released
19 Jun 2019

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

Secondary structure: helices and β-sheets

6BUT contains 11 α-helices and 5 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: 9 helices, 5 β-strands

ElementResiduesLengthSheet
α-helix3-53
α-helix6-1712
β-strand26-2831
α-helix32-387
α-helix45-5511
β-strand62-6431
α-helix65-7713
α-helix82-9211
β-strand100-10122
α-helix102-11110
α-helix118-12811
β-strand12912
β-strand135-13622
α-helix138-1469
Chain B: 2 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix1902-192019
α-helix1922-19243

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Calmodulin-1Aprotein148Homo sapiensP0DP23 (AlphaFold model)
Sodium channel protein type 2 subunit alphaBprotein31Homo sapiensQ99250 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>6BUT_1 Calmodulin-1 (chains A)
ADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGN
GTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEE
VDEMIREADIDGDGQVNYEEFVQMMTAK
Sequence of entity 2 (B), FASTA
>6BUT_2 Sodium channel protein type 2 subunit alpha (chains B)
GPGSKRKQEEVSAIIIQRAYRRYLLKQKVKK

Primary citation

Na V 1.2 EFL domain allosterically enhances Ca 2+ binding to sites I and II of WT and pathogenic calmodulin mutants bound to the channel CTD. Mahling, R., Hovey, L., Isbell, H.M. et al. Structure (2021). DOI 10.1016/j.str.2021.03.002 · 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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