cryo-EM structure of the rigor state wild type myosin-15-F-actin complex. Determined by electron microscopy at 2.83 Å resolution. Released 28 Jul 2021.
Explore 7R91 in 3D Show helices and sheets RCSB PDB PDBe
7R91 contains 103 α-helices and 78 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 | 8-12 | 5 | 1 |
| β-strand | 16-21 | 6 | 1 |
| β-strand | 29-32 | 4 | 1 |
| β-strand | 35-38 | 4 | 2 |
| β-strand | 41-42 | 2 | 3 |
| β-strand | 53-54 | 2 | 2 |
| α-helix | 56-60 | 5 | |
| β-strand | 65-68 | 4 | 2 |
| β-strand | 71-72 | 2 | 4 |
| β-strand | 75-76 | 2 | 4 |
| α-helix | 79-87 | 9 | |
| α-helix | 88-93 | 6 | |
| α-helix | 98-100 | 3 | |
| β-strand | 103-107 | 5 | 1 |
| α-helix | 113-125 | 13 | |
| β-strand | 131-136 | 6 | 1 |
| α-helix | 137-145 | 9 | |
| β-strand | 150-155 | 6 | 5 |
| β-strand | 160-166 | 7 | 5 |
| β-strand | 169-170 | 2 | 5 |
| α-helix | 172-174 | 3 | |
| β-strand | 176-178 | 3 | 5 |
| α-helix | 182-192 | 11 | |
| α-helix | 193-196 | 4 | |
| α-helix | 203-216 | 14 | |
| α-helix | 223-232 | 10 | |
| β-strand | 238-241 | 4 | 6 |
| β-strand | 247-250 | 4 | 6 |
| α-helix | 253-256 | 4 | |
| α-helix | 258-261 | 4 | |
| α-helix | 264-267 | 4 | |
| α-helix | 271-273 | 3 | |
| α-helix | 274-283 | 10 | |
| α-helix | 290-294 | 5 | |
| β-strand | 297-300 | 4 | 5 |
| α-helix | 303-305 | 3 | |
| α-helix | 309-320 | 12 | |
| β-strand | 329-330 | 2 | 5 |
| α-helix | 335-337 | 3 | |
| α-helix | 338-347 | 10 | |
| α-helix | 351-354 | 4 | |
| β-strand | 357-358 | 2 | 1 |
| α-helix | 359-365 | 7 | |
| α-helix | 366-368 | 3 | |
| α-helix | 369-373 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 8-12 | 5 | 7 |
| β-strand | 16-21 | 6 | 7 |
| β-strand | 29-32 | 4 | 7 |
| β-strand | 35-38 | 4 | 8 |
| β-strand | 53-54 | 2 | 8 |
| α-helix | 56-60 | 5 | |
| β-strand | 65-68 | 4 | 8 |
| β-strand | 71-72 | 2 | 9 |
| β-strand | 75-76 | 2 | 9 |
| α-helix | 79-87 | 9 | |
| α-helix | 88-93 | 6 | |
| α-helix | 98-100 | 3 | |
| β-strand | 103-107 | 5 | 7 |
| α-helix | 113-125 | 13 | |
| β-strand | 131-136 | 6 | 7 |
| α-helix | 137-145 | 9 | |
| β-strand | 150-155 | 6 | 3 |
| β-strand | 160-166 | 7 | 3 |
| β-strand | 169-170 | 2 | 3 |
| α-helix | 172-174 | 3 | |
| β-strand | 176-178 | 3 | 3 |
| α-helix | 182-192 | 11 | |
| α-helix | 193-196 | 4 | |
| α-helix | 203-216 | 14 | |
| α-helix | 223-232 | 10 | |
| β-strand | 238-241 | 4 | 10 |
| β-strand | 247-250 | 4 | 10 |
| α-helix | 253-256 | 4 | |
| α-helix | 258-261 | 4 | |
| α-helix | 264-267 | 4 | |
| α-helix | 271-273 | 3 | |
| α-helix | 274-283 | 10 | |
| α-helix | 290-294 | 5 | |
| β-strand | 297-300 | 4 | 3 |
| α-helix | 303-305 | 3 | |
| α-helix | 309-320 | 12 | |
| β-strand | 329-330 | 2 | 3 |
| α-helix | 335-337 | 3 | |
| α-helix | 338-347 | 10 | |
| α-helix | 351-354 | 4 | |
| β-strand | 357-358 | 2 | 7 |
| α-helix | 359-365 | 7 | |
| α-helix | 366-368 | 3 | |
| α-helix | 369-373 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 1210 | 1 | 16 |
| α-helix | 1211-1213 | 3 | |
| α-helix | 1219-1231 | 13 | |
| β-strand | 1237-1239 | 3 | 16 |
| β-strand | 1242-1246 | 5 | 16 |
| α-helix | 1257-1262 | 6 | |
| α-helix | 1275-1289 | 15 | |
| β-strand | 1293-1299 | 7 | 16 |
| α-helix | 1305-1319 | 15 | |
| α-helix | 1326-1332 | 7 | |
| α-helix | 1335-1342 | 8 | |
| β-strand | 1343-1344 | 2 | 17 |
| β-strand | 1352-1353 | 2 | 17 |
| β-strand | 1356-1364 | 9 | 16 |
| β-strand | 1367-1376 | 10 | 16 |
| β-strand | 1393 | 1 | 17 |
| α-helix | 1394-1402 | 9 | |
| α-helix | 1405-1411 | 7 | |
| α-helix | 1435-1448 | 14 | |
| α-helix | 1453-1469 | 17 | |
| β-strand | 1474-1478 | 5 | 18 |
| β-strand | 1483-1487 | 5 | 18 |
| α-helix | 1491-1500 | 10 | |
| α-helix | 1504-1512 | 9 | |
| β-strand | 1513-1517 | 5 | 19 |
| β-strand | 1522-1526 | 5 | 19 |
| α-helix | 1529-1558 | 30 | |
| β-strand | 1566-1572 | 7 | 16 |
| α-helix | 1584-1614 | 31 | |
| α-helix | 1628-1635 | 8 | |
| α-helix | 1641-1648 | 8 | |
| α-helix | 1656-1667 | 12 | |
| β-strand | 1673-1674 | 2 | 20 |
| β-strand | 1682-1687 | 6 | 20 |
| β-strand | 1690-1695 | 6 | 20 |
| β-strand | 1704 | 1 | 21 |
| α-helix | 1709-1716 | 8 | |
| α-helix | 1721-1733 | 13 | |
| β-strand | 1753 | 1 | 21 |
| α-helix | 1754-1767 | 14 | |
| β-strand | 1775-1780 | 6 | 16 |
| α-helix | 1793-1803 | 11 | |
| α-helix | 1806-1812 | 7 | |
| α-helix | 1822-1828 | 7 | |
| α-helix | 1829-1831 | 3 | |
| α-helix | 1844-1852 | 9 | |
| α-helix | 1858-1860 | 3 | |
| α-helix | 1874-1888 | 15 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Actin, alpha skeletal muscle, intermediate form | A, B, C | protein | 373 | Gallus gallus | P68139 (AlphaFold model) |
| Isoform 3 of Unconventional myosin-XV | D | protein | 685 | Mus musculus | Q9QZZ4 (AlphaFold model) |
>7R91_1 Actin, alpha skeletal muscle, intermediate form (chains A, B, C) DETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKR GILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREKMTQI MFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRLDLAG RDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEKSYEL PDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVMSGG TTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWITKQEY DEAGPSIVHRKCF
>7R91_2 Isoform 3 of Unconventional myosin-XV (chains D) EDGVEDMTQLEDLQETTVLANLKTRFERNLIYTYIGSILVSVNPYRMFAIYGPEQVQQYS GRALGENPPHLFAIANLAFAKMLDAKQNQCVIISGESGSGKTEATKLILRCLAAMNQRRD VMQQIKILEATPLLEAFGNAKTVRNDNSSRFGKFVEIFLEGGVICGAITSQYLLEKSRIV FQAKNERNYHIFYELLAGLPAQLRQAFSLQEAETYYYLNQGGNCEIAGKSDADDFRRLLA AMEVLGFTSEDQDSIFRILASILHLGNVYFEKHETDAQEVASVVSAREIQAVAELLQVSP EGLQKAITFKVTETIREKIFTPLTVESAVDARDAIAKVLYALLFGWLITRVNALVSPKQD TLSIAILDIYGFEDLSFNSFEQLCINYANENLQYLFNKIVFQEEQEEYIREQMDWREIAF ADNQPCINLISLKPYGILRILDDQCCFPQATDHTFLQKCHYHHGANPLYSKPKMPLPEFT IKHYAGKVTYQVHKFLDKNHDQVRQDVLDLFVHSRTRVVAHLFSSHAAQTAPPRLGKSSS ITRLYKAHTVAAKFQQSLLDLVEKMERCNPLFVRCLKPNHKKEPGLFEPDVMMAQLRYSG VLETVRIRKEGFPVRLPFQVFIDRYRCLVALKLNVPADGDMCVSLLSRLCTVTPDMYRVG ISKLFLKEHLHQLLESMRERVQNRA
Structural basis for tunable control of actin dynamics by myosin-15 in mechanosensory stereocilia. Gong, R., Jiang, F., Moreland, Z.G. et al. Sci Adv (2022) 8:eabl4733-eabl4733. DOI 10.1126/sciadv.abl4733 · PubMed
Other PDB entries of the same protein (UniProt P68139 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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