cryo-EM structure of cardiac muscle alpha-actin M305L hcm mutant. Determined by electron microscopy at 3.12 Å resolution. Released 14 May 2025.
Explore 9BPH in 3D Show helices and sheets RCSB PDB PDBe
9BPH contains 96 α-helices and 76 β-strands across 4 chains. 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 |
|---|---|---|---|
| β-strand | 8-11 | 4 | 1 |
| β-strand | 17-21 | 5 | 1 |
| β-strand | 29-31 | 3 | 1 |
| β-strand | 35-38 | 4 | 2 |
| β-strand | 53-54 | 2 | 2 |
| α-helix | 56-60 | 5 | |
| β-strand | 65-68 | 4 | 2 |
| β-strand | 71-72 | 2 | 3 |
| β-strand | 75-76 | 2 | 3 |
| α-helix | 79-87 | 9 | |
| α-helix | 88-92 | 5 | |
| α-helix | 98-100 | 3 | |
| β-strand | 103-107 | 5 | 1 |
| α-helix | 113-122 | 10 | |
| α-helix | 123-127 | 5 | |
| β-strand | 131-136 | 6 | 1 |
| α-helix | 137-144 | 8 | |
| β-strand | 150-155 | 6 | 4 |
| β-strand | 160-166 | 7 | 4 |
| β-strand | 169-170 | 2 | 4 |
| α-helix | 172-174 | 3 | |
| β-strand | 176-178 | 3 | 4 |
| α-helix | 182-193 | 12 | |
| α-helix | 194-196 | 3 | |
| α-helix | 203-205 | 3 | |
| α-helix | 206-216 | 11 | |
| α-helix | 224-232 | 9 | |
| β-strand | 238-242 | 5 | 5 |
| β-strand | 245-250 | 6 | 5 |
| α-helix | 252-254 | 3 | |
| α-helix | 258-261 | 4 | |
| α-helix | 264-266 | 3 | |
| α-helix | 274-283 | 10 | |
| α-helix | 290-294 | 5 | |
| β-strand | 297-300 | 4 | 4 |
| α-helix | 302-304 | 3 | |
| α-helix | 309-320 | 12 | |
| β-strand | 329-330 | 2 | 4 |
| α-helix | 338-346 | 9 | |
| α-helix | 350-354 | 5 | |
| β-strand | 357-358 | 2 | 1 |
| α-helix | 359-365 | 7 | |
| α-helix | 369-373 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Actin, alpha cardiac muscle 1 | A, B, C, D | protein | 375 | Homo sapiens | P68032 (AlphaFold model) |
>9BPH_1 Actin, alpha cardiac muscle 1 (chains A, B, C, D) DDEETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQS KRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREKMT QIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRLDL AGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEKSY ELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVLS GGTTLYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQ EYDEAGPSIVHRKCF
CRYO-EM STRUCTURE OF CARDIAC MUSCLE ALPHA-ACTIN M305L HCM MUTANT. Huang, H.L., Heissler, S.M., Chinthalapudi, K. To be published.
Other PDB entries of the same protein (UniProt P68032 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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