4JPZ: Fibroblast growth factor 13

Voltage-gated sodium channel 1.2 C-terminal domain in complex with FGF13U and Ca2+/calmodulin. Determined by X-ray diffraction at 3.02 Å resolution. Released 16 Apr 2014.

Method
X-ray diffraction
Resolution
3.02 Å
Organism
Homo sapiens
Chains
6
Atoms
6,991
Mol. weight
119.32 kDa
Ligands
CA
Released
16 Apr 2014

Explore 4JPZ in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4JPZ contains 44 α-helices and 47 β-strands across 6 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: 7 helices, 15 β-strands

ElementResiduesLengthSheet
β-strand13-22101
β-strand27-3041
β-strand36-3941
α-helix45-473
β-strand49-5571
β-strand58-6361
β-strand68-7251
β-strand78-8141
β-strand8412
α-helix86-883
β-strand90-9561
β-strand99-108101
β-strand115-11731
β-strand12013
α-helix1251
β-strand12613
α-helix127-1282
α-helix129-1313
α-helix137-1393
β-strand141-151111
α-helix152-1543
β-strand15612
Chain B: 7 helices, 4 β-strands
ElementResiduesLengthSheet
α-helix1792-180514
β-strand1812-181434
α-helix1818-18236
α-helix18321
α-helix1836-18394
β-strand1845-184734
β-strand1851-185334
α-helix1854-186613
α-helix1870-188617
β-strand1898-189924
α-helix1900-192627
Chain C: 9 helices, 4 β-strands
ElementResiduesLengthSheet
α-helix10-2011
β-strand2815
α-helix30-4011
α-helix46-549
β-strand6415
α-helix66-7712
α-helix87-915
β-strand100-10236
α-helix103-11210
α-helix116-1183
α-helix119-12911
β-strand136-13836
α-helix139-1468
Chain E: 5 helices, 16 β-strands
ElementResiduesLengthSheet
β-strand12-22117
β-strand26-3057
β-strand36-3947
α-helix45-473
β-strand49-5577
β-strand58-6367
β-strand68-7257
β-strand78-8147
β-strand8418
α-helix86-883
β-strand89-9577
β-strand99-108107
β-strand115-11737
β-strand12019
β-strand12517
β-strand12619
α-helix127-1282
α-helix129-1313
α-helix137-1393
β-strand141-152127
β-strand15618
Chain H: 7 helices, 4 β-strands
ElementResiduesLengthSheet
α-helix1792-180514
β-strand1812-1814310
α-helix1815-18239
α-helix18321
α-helix1836-18394
β-strand1845-1847310
β-strand1851-1853310
α-helix1854-186613
α-helix1870-188617
β-strand1896-1899410
α-helix1900-192728
Chain I: 9 helices, 4 β-strands
ElementResiduesLengthSheet
α-helix9-2012
β-strand28111
α-helix30-4011
α-helix46-549
β-strand64111
α-helix66-7712
α-helix87-915
β-strand100-102312
α-helix103-11210
α-helix116-1183
α-helix119-12911
β-strand136-138312
α-helix139-1479

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Fibroblast growth factor 13A, Eprotein192Homo sapiensQ92913 (AlphaFold model)
Sodium channel protein type 2 subunit alphaB, Hprotein184Homo sapiensQ99250 (AlphaFold model)
CalmodulinC, Iprotein149Homo sapiensP0DP23 (AlphaFold model)
Sequence of entity 1 (A, E), FASTA
>4JPZ_1 Fibroblast growth factor 13 (chains A, E)
MALLRKSYSEPQLKGIVTKLYSRQGYHLQLQADGTIDGTKDEDSTYTLFNLIPVGLRVVA
IQGVQTKLYLAMNSEGYLYTSELFTPECKFKESVFENYYVTYSSMIYRQQQSGRGWYLGL
NKEGEIMKGNHVKKNKPAAHFLPKPLKVAMYKEPSLHDLTEFSRSGSGTPTKSRSVSGVL
NGGKSMSHNEST
Sequence of entity 2 (B, H), FASTA
>4JPZ_2 Sodium channel protein type 2 subunit alpha (chains B, H)
MGSSHHHHHHSSGLVPRGSHMASENFSVATEESAEPLSEDDFEMFYEVWEKFDPDATQFI
EFAKLSDFADALDPPLLIAKPNKVQLIAMDLPMVSGDRIHCLDILFAFTKRVLGESGEMD
ALRIQMEERFMASNPSKVSYEPITTTLKRKQEEVSAIIIQRAYRRYLLKQKVKKVSSIYK
KDKG
Sequence of entity 3 (C, I), FASTA
>4JPZ_3 Calmodulin (chains C, I)
MADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADG
NGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDE
EVDEMIREADIDGDGQVNYEEFVQMMTAK

Ligands and cofactors

IDNameFormulaCopies
CACalcium ionCa8

Primary citation

Structural analyses of Ca(2+)/CaM interaction with NaV channel C-termini reveal mechanisms of calcium-dependent regulation. Wang, C., Chung, B.C., Yan, H. et al. Nat Commun (2014) 5:4896-4896. DOI 10.1038/ncomms5896 · PubMed

Other PDB entries of the same protein (UniProt Q92913 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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