8QYR: Myosin-7

Beta-cardiac myosin motor domain in the pre-powerstroke state complexed to Mavacamten. Determined by X-ray diffraction at 1.8 Å resolution. Released 13 Dec 2023.

Method
X-ray diffraction
Resolution
1.8 Å
Organism
Bos taurus
Chains
1
Atoms
6,258
Mol. weight
90.34 kDa
Ligands
BEF, ADP, MG, XB2
Released
13 Dec 2023

Explore 8QYR in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8QYR contains 38 α-helices and 28 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 B: 38 helices, 28 β-strands

ElementResiduesLengthSheet
β-strand36-4161
β-strand45-55111
β-strand58-6361
β-strand68-7251
α-helix73-753
β-strand77-7821
α-helix79-813
α-helix82-843
β-strand8912
α-helix90-923
α-helix98-11013
β-strand115-11842
β-strand121-12552
α-helix136-1427
α-helix147-1493
α-helix154-16815
β-strand172-17762
β-strand17913
α-helix184-20118
α-helix216-23116
β-strand232-23324
β-strand241-24224
β-strand245-25282
β-strand258-26692
α-helix270-2734
β-strand28314
α-helix284-2907
α-helix295-3006
α-helix307-3093
α-helix311-3133
α-helix325-33814
α-helix343-35917
β-strand364-36635
β-strand373-37535
α-helix379-3879
α-helix392-4009
β-strand403-40646
β-strand409-41246
α-helix417-44731
β-strand455-46172
α-helix462-4643
β-strand46513
α-helix473-49018
α-helix491-4966
α-helix497-5037
α-helix518-5258
α-helix530-5378
α-helix545-55612
β-strand563-56427
β-strand577-58157
β-strand584-58857
α-helix593-5986
α-helix603-6108
α-helix615-6206
α-helix647-66317
β-strand666-67382
α-helix686-69510
α-helix698-70710
β-strand711-71448
α-helix715-7228
α-helix723-7253
α-helix727-7293
α-helix738-74710
β-strand756-75838
β-strand762-76548
α-helix769-78012

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Myosin-7Bprotein781Bos taurusQ9BE39 (AlphaFold model)
Sequence of entity 1 (B), FASTA
>8QYR_1 Myosin-7 (chains B)
MVDAEMAAFGEAAPYLRKSEKERLEAQTRPFDLKKDVFVPDDKEEFVKATILSREGGKVT
AETEHGKTVTVKEDQVLQQNPPKFDKIEDMAMLTFLHEPAVLYNLKERYASWMIYTYSGL
FCVTINPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGES
GAGKTVNTKRVIQYFAVIAAIGDRSKKEQATGKGTLEDQIIQANPALEAFGNAKTVRNDN
SSRFGKFIRIHFGATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDM
LLITNNPYDYAFISQGETTVASIDDAEELMATDNAFDVLGFTTEEKNSMYKLTGAIMHFG
NMKFKLKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQQV
VYAKGALAKAVYERMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINF
TNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMF
PKATDMTFKAKLFDNHLGKSSNFQKPRNIKGKPEAHFSLIHYAGTVDYNIIGWLQKNKDP
LNETVVDLYKKSSLKMLSSLFANYAGFDTPIEKGKGKAKKGSSFQTVSALHRENLNKLMT
NLRSTHPHFVRCIIPNETKSPGVIDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQ
RYRILNPAAIPEGQDIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFKAGLLGLLEEMRDER
L

Ligands and cofactors

IDNameFormulaCopies
BEFBeryllium trifluoride ionBe F31
ADPAdenosine-5'-diphosphateC10 H15 N5 O10 P21
MGMagnesium ionMg1
XB2MavacamtenC15 H19 N3 O21

Water and common crystallization additives (EDO, SO4) are not listed.

Primary citation

Omecamtiv mecarbil and Mavacamten target the same myosin pocket despite antagonistic effects in heart contraction. Auguin, D., Robert-Paganin, J., Rety, S. et al. bioRxiv (2023). DOI 10.1101/2023.11.15.567213 · 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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