9HTF: Myosin-7

Beta-cardiac myosin Y115H mutant motor domain in the pre-powerstroke state, MgADP.VO4 form. Determined by X-ray diffraction at 2.48 Å resolution. Released 22 Oct 2025.

Method
X-ray diffraction
Resolution
2.48 Å
Organism
Homo sapiens
Chains
1
Atoms
5,706
Mol. weight
94.14 kDa
Ligands
VO4, ADP, MG
Released
22 Oct 2025

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

Secondary structure: helices and β-sheets

9HTF contains 37 α-helices and 26 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: 37 helices, 26 β-strands

ElementResiduesLengthSheet
β-strand37-3931
β-strand47-4821
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-helix271-2744
β-strand28314
α-helix284-2896
α-helix295-3017
α-helix307-3093
α-helix311-3133
α-helix325-33814
α-helix343-36018
β-strand364-36635
β-strand373-37535
α-helix379-38810
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-helix530-5389
α-helix545-55612
β-strand563-56427
β-strand577-58157
β-strand584-58857
α-helix593-5986
α-helix603-6119
α-helix615-6206
α-helix647-66317
β-strand666-67382
α-helix686-69611
α-helix698-70710
β-strand711-71448
α-helix715-7228
α-helix723-7253
α-helix738-74811
β-strand756-75838
β-strand762-76548
α-helix7661
α-helix769-77810

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Myosin-7Aprotein819Homo sapiensP12883 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>9HTF_1 Myosin-7 (chains A)
MGDSEMAVFGAAAPYLRKSEKERLEAQTRPFDLKKDVFVPDDKQEFVKAKIVSREGGKVT
AETEYGKTVTVKEDQVMQQNPPKFDKIEDMAMLTFLHEPAVLYNLKDRYGSWMIHTYSGL
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 (EDO, GOL) 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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