9I8P: Myosin-7

Human beta-cardiac myosin wild type motor domain in the pre-powerstroke state, MgADP.VO4 form. Determined by X-ray diffraction at 2.6 Å resolution. Released 22 Oct 2025.

Method
X-ray diffraction
Resolution
2.6 Å
Organism
Homo sapiens
Chains
1
Atoms
5,816
Mol. weight
94.36 kDa
Ligands
VO4, ADP, MG
Released
22 Oct 2025

Explore 9I8P in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9I8P contains 39 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 A: 39 helices, 28 β-strands

ElementResiduesLengthSheet
β-strand3711
β-strand38-4142
β-strand45-4842
β-strand7811
α-helix79-813
α-helix82-843
β-strand8913
α-helix90-923
α-helix98-11013
β-strand115-11843
β-strand121-12553
α-helix136-1427
α-helix147-1493
α-helix154-16815
β-strand172-17763
β-strand17914
α-helix184-19916
α-helix216-23116
β-strand232-23325
β-strand241-24225
β-strand245-25283
β-strand258-26693
α-helix271-2744
β-strand28315
α-helix284-2907
α-helix295-3017
α-helix307-3093
α-helix325-33814
α-helix343-36119
β-strand364-36636
β-strand373-37536
α-helix379-38810
α-helix392-4009
β-strand403-40647
β-strand409-41247
α-helix413-4142
α-helix417-44731
β-strand455-46173
α-helix462-4643
β-strand46514
β-strand47118
α-helix473-49018
α-helix491-4966
α-helix497-5037
α-helix518-5258
α-helix530-5378
α-helix545-55612
β-strand563-56428
α-helix572-5743
β-strand577-58158
β-strand584-58858
α-helix593-5986
α-helix603-6108
α-helix615-6206
α-helix628-6303
α-helix647-66317
β-strand666-67383
α-helix686-69611
α-helix698-70710
β-strand711-71449
α-helix715-7228
α-helix723-7253
α-helix727-7293
α-helix738-74710
β-strand756-75839
β-strand762-76549
α-helix769-77911

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Myosin-7Aprotein819Homo sapiensP12883 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>9I8P_1 Myosin-7 (chains A)
MGDSEMAVFGAAAPYLRKSEKERLEAQTRPFDLKKDVFVPDDKQEFVKAKIVSREGGKVT
AETEYGKTVTVKEDQVMQQNPPKFDKIEDMAMLTFLHEPAVLYNLKDRYGSWMIYTYSGL
FCVTVNPYKWLPVYTPEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGES
GAGKTVNTKRVIQYFAVIAAIGDRSKKDQSPGKGTLEDQIIQANPALEAFGNAKTVRNDN
SSRFGKFIRIHFGATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDM
LLITNNPYDYAFISQGETTVASIDDAEELMATDNAFDVLGFTSEEKNSMYKLTGAIMHFG
NMKFKLKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQQV
IYATGALAKAVYERMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINF
TNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMF
PKATDMTFKAKLFDNHLGKSANFQKPRNIKGKPEAHFSLIHYAGIVDYNIIGWLQKNKDP
LNETVVGLYQKSSLKLLSTLFANYAGADAPIEKGKGKAKKGSSFQTVSALHRENLNKLMT
NLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQ
RYRILNPAAIPEGQFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFKAGLLGLLEEMRDER
LSRIITRIQAQSRGVLARMEYKKLLERRGSGRGSIDTWV

Ligands and cofactors

IDNameFormulaCopies
VO4Vanadate ionO4 V1
ADPAdenosine-5'-diphosphateC10 H15 N5 O10 P21
MGMagnesium ionMg1

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

Primary citation

Hypertrophic cardiomyopathy mutations Y115H and E497D disrupt the folded-back state of human beta-cardiac myosin allosterically. Nandwani, N., Bhowmik, D., Glaser, C. et al. Nat Commun (2025) 16:8751-8751. DOI 10.1038/s41467-025-63816-1 · PubMed

Other PDB entries of the same protein (UniProt P12883 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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