Beta-cardiac heavy meromyosin motor domain in the primed state complexed to mavacamten. Determined by electron microscopy at 2.9 Å resolution. Released 12 Mar 2025.
Explore 9GZ2 in 3D Show helices and sheets RCSB PDB PDBe
9GZ2 contains 39 α-helices and 30 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 4-15 | 12 | |
| α-helix | 20-26 | 7 | |
| β-strand | 36-40 | 5 | 1 |
| β-strand | 46-55 | 10 | 1 |
| β-strand | 58-63 | 6 | 1 |
| β-strand | 68-72 | 5 | 1 |
| β-strand | 77-78 | 2 | 1 |
| α-helix | 79-81 | 3 | |
| α-helix | 82-84 | 3 | |
| β-strand | 89 | 1 | 2 |
| α-helix | 90-92 | 3 | |
| α-helix | 98-109 | 12 | |
| β-strand | 115-117 | 3 | 2 |
| β-strand | 122-125 | 4 | 2 |
| α-helix | 136-142 | 7 | |
| α-helix | 151-152 | 2 | |
| α-helix | 154-168 | 15 | |
| β-strand | 172-177 | 6 | 2 |
| β-strand | 179 | 1 | 3 |
| α-helix | 184-201 | 18 | |
| α-helix | 215-231 | 17 | |
| β-strand | 232-233 | 2 | 4 |
| β-strand | 241-242 | 2 | 4 |
| β-strand | 246-252 | 7 | 2 |
| β-strand | 258-265 | 8 | 2 |
| α-helix | 270-273 | 4 | |
| β-strand | 283 | 1 | 4 |
| α-helix | 284-291 | 8 | |
| α-helix | 295-300 | 6 | |
| α-helix | 307-309 | 3 | |
| α-helix | 311-314 | 4 | |
| α-helix | 325-338 | 14 | |
| α-helix | 343-359 | 17 | |
| β-strand | 363-366 | 4 | 5 |
| β-strand | 373-377 | 5 | 5 |
| α-helix | 379-387 | 9 | |
| α-helix | 392-400 | 9 | |
| β-strand | 403-406 | 4 | 6 |
| β-strand | 409-412 | 4 | 6 |
| α-helix | 414-416 | 3 | |
| α-helix | 417-443 | 27 | |
| β-strand | 448 | 1 | 2 |
| β-strand | 455-461 | 7 | 2 |
| α-helix | 462-464 | 3 | |
| β-strand | 465 | 1 | 3 |
| β-strand | 471 | 1 | 7 |
| α-helix | 473-490 | 18 | |
| α-helix | 491-495 | 5 | |
| α-helix | 496-503 | 8 | |
| α-helix | 518-525 | 8 | |
| α-helix | 530-537 | 8 | |
| α-helix | 545-556 | 12 | |
| β-strand | 563-564 | 2 | 7 |
| β-strand | 577-581 | 5 | 7 |
| β-strand | 584-588 | 5 | 7 |
| α-helix | 593-598 | 6 | |
| α-helix | 603-610 | 8 | |
| α-helix | 615-620 | 6 | |
| α-helix | 647-663 | 17 | |
| β-strand | 666-673 | 8 | 2 |
| α-helix | 686-695 | 10 | |
| α-helix | 698-707 | 10 | |
| β-strand | 711-714 | 4 | 8 |
| α-helix | 715-722 | 8 | |
| α-helix | 723-725 | 3 | |
| α-helix | 738-748 | 11 | |
| β-strand | 756-758 | 3 | 8 |
| β-strand | 762-765 | 4 | 8 |
| α-helix | 769-794 | 26 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Myosin-7 | A | protein | 1145 | Homo sapiens | P12883 (AlphaFold model) |
>9GZ2_1 Myosin-7 (chains A) GDSEMAVFGAAAPYLRKSEKERLEAQTRPFDLKKDVFVPDDKQEFVKAKIVSREGGKVTA ETEYGKTVTVKEDQVMQQNPPKFDKIEDMAMLTFLHEPAVLYNLKDRYGSWMIYTYSGLF CVTVNPYKWLPVYTPEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGESG AGKTVNTKRVIQYFAVIAAIGDRSKKDQSPGKGTLEDQIIQANPALEAFGNAKTVRNDNS SRFGKFIRIHFGATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDML LITNNPYDYAFISQGETTVASIDDAEELMATDNAFDVLGFTSEEKNSMYKLTGAIMHFGN MKFKLKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQQVI YATGALAKAVYERMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFT NEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFP KATDMTFKAKLFDNHLGKSANFQKPRNIKGKPEAHFSLIHYAGIVDYNIIGWLQKNKDPL NETVVGLYQKSSLKLLSTLFANYAGADAPIEKGKGKAKKGSSFQTVSALHRENLNKLMTN LRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQR YRILNPAAIPEGQFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFKAGLLGLLEEMRDERL SRIITRIQAQSRGVLARMEYKKLLERRDSLLVIQWNIRAFMGVKNWPWMKLYFKIKPLLK SAEREKEMASMKEEFTRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADA EERCDQLIKNKIQLEAKVKEMNERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTL AKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLT KAKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKQQLDERLK KKDFELNALNARIEDEQALGSQLQKKLKELQARIEELEEELESERTARAKVEKLRSDDYK DDDDK
| ID | Name | Formula | Copies |
|---|---|---|---|
| XB2 | Mavacamten | C15 H19 N3 O2 | 1 |
| PO4 | Phosphate ion | O4 P | 1 |
| ADP | Adenosine-5'-diphosphate | C10 H15 N5 O10 P2 | 1 |
| MG | Magnesium ion | Mg | 1 |
Mavacamten inhibits myosin activity by stabilising the myosin interacting-heads motif and stalling motor force generation. McMillan, S.N., Pitts, J.R.T., Barua, B. et al. bioRxiv (2025). DOI 10.1101/2025.02.12.637875 · PubMed
Other PDB entries of the same protein (UniProt P12883 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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