6MC9: Human Nav1.4 C-Terminal (1599-1754) domain

Crystal Structure of Human Nav1.4 C-Terminal (1599-1754) domain in complex with calcium-bound calmodulin. Determined by X-ray diffraction at 3.3 Å resolution. Released 10 Apr 2019.

Method
X-ray diffraction
Resolution
3.3 Å
Organisms
Homo sapiens, Rattus norvegicus
Chains
2
Atoms
2,330
Mol. weight
36.22 kDa
Ligands
CA
Released
10 Apr 2019

Explore 6MC9 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6MC9 contains 14 α-helices and 8 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: 6 helices, 4 β-strands

ElementResiduesLengthSheet
α-helix1614-162714
β-strand1634-163631
α-helix1637-16459
α-helix1658-16647
β-strand1667-166931
β-strand1673-167531
α-helix1676-168712
α-helix1692-170817
β-strand1719-172021
α-helix1721-175939
Chain B: 8 helices, 4 β-strands
ElementResiduesLengthSheet
α-helix12-198
β-strand2712
α-helix29-3911
α-helix45-5410
β-strand6312
α-helix65-7612
α-helix82-9211
β-strand99-10133
α-helix102-1109
α-helix118-12811
β-strand135-13733
α-helix138-1458

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Sodium channel protein type 4 subunit alphaAprotein168Homo sapiensP35499 (AlphaFold model)
Calmodulin-1Bprotein149Rattus norvegicusP0DP29 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>6MC9_1 Sodium channel protein type 4 subunit alpha (chains A)
GPLGSENFNVATEESSEPLGEDDFEMFYETWEKFDPDATQFIAYSRLSDFVDTLQEPLRI
AKPNKIKLITLDLPMVPGDKIHCLDILFALTKEVLGDSGEMDALKQTMEEKFMAANPSKV
SYEPITTTLKRKHEEVCAIKIQRAYRRHLLQRSMKQASYMYLTRAAAS
Sequence of entity 2 (B), FASTA
>6MC9_2 Calmodulin-1 (chains B)
MADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADG
NGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDE
EVDEMIREADIDGDGQVNYEEFVQMMTAK

Ligands and cofactors

IDNameFormulaCopies
CACalcium ionCa4

Primary citation

Ca2+-dependent regulation of sodium channels NaV1.4 and NaV1.5 is controlled by the post-IQ motif. Yoder, J.B., Ben-Johny, M., Farinelli, F. et al. Nat Commun (2019) 10:1514-1514. DOI 10.1038/s41467-019-09570-7 · PubMed

Other PDB entries of the same protein (UniProt P35499 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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