5N6A: Myosin-7

Cardiac muscle myosin motor domain in the pre-powerstroke state. Determined by X-ray diffraction at 3.1 Å resolution. Released 9 Aug 2017.

Method
X-ray diffraction
Resolution
3.1 Å
Organism
Bos taurus
Chains
1
Atoms
5,569
Mol. weight
95.43 kDa
Ligands
ADP, PO4, MG
Released
9 Aug 2017

Explore 5N6A in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5N6A contains 28 α-helices and 29 β-strands across 1 chain. 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: 28 helices, 29 β-strands

ElementResiduesLengthSheet
β-strand36-4051
β-strand46-5051
β-strand51-5442
β-strand58-6032
β-strand6912
β-strand78-7921
α-helix801
β-strand8913
α-helix90-923
α-helix98-10912
β-strand115-11733
β-strand122-12543
α-helix136-1427
α-helix154-16714
β-strand172-17873
β-strand17914
α-helix184-19613
α-helix219-2235
α-helix224-2263
β-strand232-23325
β-strand241-24225
β-strand246-25273
β-strand258-26583
α-helix270-2723
β-strand28315
α-helix284-2918
α-helix325-33814
α-helix343-35917
β-strand365-36846
β-strand372-37436
α-helix383-3864
α-helix393-4008
β-strand403-40647
β-strand409-41247
α-helix4131
α-helix417-44731
β-strand456-46163
β-strand46514
α-helix473-49321
α-helix496-5049
α-helix518-5247
α-helix530-53910
α-helix545-55612
β-strand563-56428
β-strand577-57938
β-strand586-58838
α-helix594-5974
α-helix603-6108
α-helix615-6228
α-helix647-66216
β-strand666-67383
α-helix686-6894
α-helix692-6965
β-strand711-71229
β-strand756-75729
β-strand764-76529
α-helix767-7748

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Myosin-7Aprotein828Bos taurusQ9BE39 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>5N6A_1 Myosin-7 (chains A)
MVDAEMAAFGEAAPYLRKSEKERLEAQTRPFDLKKDVFVPDDKEEFVKATILSREGGKVT
AETEHGKTVTVKEDQVLQQNPPKFDKIEDMAMLTFLHEPAVLYNLKERYASWMIYTYSGL
FCVTINPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGES
GAGKTVNTKRVIQYFAVIAAIGDRSKKEQATGKGTLEDQIIQANPALEAFGNAKTVRNDN
SSRFGKFIRIHFGATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDM
LLITNNPYDYAFISQGETTVASIDDAEELMATDNAFDVLGFTTEEKNSMYKLTGAIMHFG
NMKFKLKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQQV
VYAKGALAKAVYERMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINF
TNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMF
PKATDMTFKAKLFDNHLGKSSNFQKPRNIKGKPEAHFSLIHYAGTVDYNIIGWLQKNKDP
LNETVVDLYKKSSLKMLSSLFANYAGFDTPIEKGKGKAKKGSSFQTVSALHRENLNKLMT
NLRSTHPHFVRCIIPNETKSPGVIDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQ
RYRILNPAAIPEGQFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFKAGLLGLLEEMRDER
LSRIITRIQAQSRGVLSRMEFKKLLERRDSLLIIQWNIRAFMGVKNWP

Ligands and cofactors

IDNameFormulaCopies
ADPAdenosine-5'-diphosphateC10 H15 N5 O10 P21
PO4Phosphate ionO4 P1
MGMagnesium ionMg1

Water and common crystallization additives (GOL) are not listed.

Primary citation

Mechanistic and structural basis for activation of cardiac myosin force production by omecamtiv mecarbil. Planelles-Herrero, V.J., Hartman, J.J., Robert-Paganin, J. et al. Nat Commun (2017) 8:190-190. DOI 10.1038/s41467-017-00176-5 · PubMed

Other PDB entries of the same protein (UniProt Q9BE39 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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