cryo-EM structure of the ADP state wild type myosin-15-F-actin complex (symmetry expansion and re-centering). Determined by electron microscopy at 4.15 Å resolution. Released 3 Aug 2022.
Explore 7UDU in 3D Show helices and sheets RCSB PDB PDBe
7UDU contains 114 α-helices and 84 β-strands across 5 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 |
|---|---|---|---|
| α-helix | 6-7 | 2 | |
| 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 | 1 | 2 |
| α-helix | 55-60 | 6 | |
| α-helix | 62-64 | 3 | |
| 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 | 88-92 | 5 | |
| α-helix | 98-100 | 3 | |
| β-strand | 103-107 | 5 | 1 |
| α-helix | 113-125 | 13 | |
| β-strand | 131-136 | 6 | 1 |
| α-helix | 137-144 | 8 | |
| β-strand | 149-155 | 7 | 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 | 182-193 | 12 | |
| α-helix | 194-196 | 3 | |
| α-helix | 203-216 | 14 | |
| α-helix | 223-230 | 8 | |
| β-strand | 238-241 | 4 | 6 |
| β-strand | 247-250 | 4 | 6 |
| α-helix | 253-256 | 4 | |
| α-helix | 258-261 | 4 | |
| α-helix | 274-282 | 9 | |
| α-helix | 287-295 | 9 | |
| β-strand | 297-300 | 4 | 5 |
| α-helix | 302-304 | 3 | |
| α-helix | 309-320 | 12 | |
| α-helix | 326-327 | 2 | |
| β-strand | 329-330 | 2 | 5 |
| α-helix | 338-348 | 11 | |
| α-helix | 350-355 | 6 | |
| β-strand | 357-358 | 2 | 1 |
| α-helix | 359-365 | 7 | |
| α-helix | 367-371 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 6-7 | 2 | |
| 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 | 1 | 8 |
| α-helix | 55-60 | 6 | |
| α-helix | 62-64 | 3 | |
| 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 | 88-92 | 5 | |
| α-helix | 98-100 | 3 | |
| β-strand | 103-107 | 5 | 7 |
| α-helix | 113-125 | 13 | |
| β-strand | 131-136 | 6 | 7 |
| α-helix | 137-144 | 8 | |
| β-strand | 149-155 | 7 | 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 | 182-193 | 12 | |
| α-helix | 194-196 | 3 | |
| α-helix | 203-216 | 14 | |
| α-helix | 223-230 | 8 | |
| β-strand | 238-241 | 4 | 10 |
| β-strand | 247-250 | 4 | 10 |
| α-helix | 253-256 | 4 | |
| α-helix | 258-261 | 4 | |
| α-helix | 274-282 | 9 | |
| α-helix | 287-295 | 9 | |
| β-strand | 297-300 | 4 | 3 |
| α-helix | 302-304 | 3 | |
| α-helix | 309-320 | 12 | |
| α-helix | 326-327 | 2 | |
| β-strand | 329-330 | 2 | 3 |
| α-helix | 338-348 | 11 | |
| α-helix | 350-355 | 6 | |
| β-strand | 357-358 | 2 | 7 |
| α-helix | 359-365 | 7 | |
| α-helix | 367-371 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 1211-1213 | 3 | |
| α-helix | 1219-1231 | 13 | |
| β-strand | 1237-1239 | 3 | 16 |
| β-strand | 1242-1246 | 5 | 16 |
| α-helix | 1258-1262 | 5 | |
| α-helix | 1265-1267 | 3 | |
| α-helix | 1272-1273 | 2 | |
| α-helix | 1277-1289 | 13 | |
| β-strand | 1293-1299 | 7 | 16 |
| α-helix | 1305-1317 | 13 | |
| α-helix | 1332-1334 | 3 | |
| α-helix | 1335-1342 | 8 | |
| β-strand | 1343-1346 | 4 | 17 |
| β-strand | 1349-1353 | 5 | 17 |
| β-strand | 1358-1364 | 7 | 16 |
| β-strand | 1367-1374 | 8 | 16 |
| α-helix | 1381-1384 | 4 | |
| β-strand | 1393 | 1 | 17 |
| α-helix | 1394-1401 | 8 | |
| α-helix | 1405-1410 | 6 | |
| α-helix | 1420-1423 | 4 | |
| α-helix | 1436-1448 | 13 | |
| α-helix | 1453-1470 | 18 | |
| β-strand | 1474 | 1 | 18 |
| β-strand | 1478 | 1 | 19 |
| β-strand | 1483 | 1 | 19 |
| β-strand | 1487 | 1 | 18 |
| α-helix | 1490-1498 | 9 | |
| α-helix | 1504-1512 | 9 | |
| β-strand | 1513-1517 | 5 | 20 |
| β-strand | 1522-1526 | 5 | 20 |
| α-helix | 1529-1558 | 30 | |
| β-strand | 1566-1572 | 7 | 16 |
| β-strand | 1582 | 1 | 21 |
| α-helix | 1584-1615 | 32 | |
| α-helix | 1617-1619 | 3 | |
| α-helix | 1628-1635 | 8 | |
| α-helix | 1641-1650 | 10 | |
| α-helix | 1656-1666 | 11 | |
| β-strand | 1673-1674 | 2 | 21 |
| β-strand | 1682-1687 | 6 | 21 |
| β-strand | 1690-1695 | 6 | 21 |
| α-helix | 1700-1702 | 3 | |
| β-strand | 1704 | 1 | 22 |
| α-helix | 1709-1716 | 8 | |
| α-helix | 1721-1733 | 13 | |
| β-strand | 1753 | 1 | 22 |
| α-helix | 1754-1771 | 18 | |
| β-strand | 1773-1774 | 2 | 16 |
| β-strand | 1777-1780 | 4 | 16 |
| α-helix | 1793-1803 | 11 | |
| α-helix | 1807-1812 | 6 | |
| α-helix | 1823-1828 | 6 | |
| α-helix | 1847-1854 | 8 | |
| α-helix | 1872-1906 | 35 | |
| α-helix | 1907-1911 | 5 | |
| α-helix | 1914-1921 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 28-41 | 14 | |
| α-helix | 51-59 | 9 | |
| α-helix | 83-92 | 10 | |
| α-helix | 100-108 | 9 | |
| β-strand | 118-119 | 2 | 23 |
| α-helix | 120-129 | 10 | |
| α-helix | 133-135 | 3 | |
| α-helix | 136-145 | 10 | |
| β-strand | 148 | 1 | 23 |
| β-strand | 153-154 | 2 | 23 |
| α-helix | 157-165 | 9 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Actin, alpha skeletal muscle | A, B, C | protein | 373 | Gallus gallus | P68139 (AlphaFold model) |
| Unconventional myosin-XV | D | protein | 719 | Mus musculus | Q9QZZ4 (AlphaFold model) |
| regulatory light chain | E | protein | 146 | Gallus gallus | P24032 (AlphaFold model) |
>7UDU_1 Actin, alpha skeletal muscle (chains A, B, C) DETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKR GILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREKMTQI MFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRLDLAG RDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEKSYEL PDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVMSGG TTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWITKQEY DEAGPSIVHRKCF
>7UDU_2 Unconventional myosin-XV (chains D) EDGVEDMTQLEDLQETTVLANLKTRFERNLIYTYIGSILVSVNPYRMFAIYGPEQVQQYS GRALGENPPHLFAIANLAFAKMLDAKQNQCVIISGESGSGKTEATKLILRCLAAMNQRRD VMQQIKILEATPLLEAFGNAKTVRNDNSSRFGKFVEIFLEGGVICGAITSQYLLEKSRIV FQAKNERNYHIFYELLAGLPAQLRQAFSLQEAETYYYLNQGGNCEIAGKSDADDFRRLLA AMEVLGFTSEDQDSIFRILASILHLGNVYFEKHETDAQEVASVVSAREIQAVAELLQVSP EGLQKAITFKVTETIREKIFTPLTVESAVDARDAIAKVLYALLFGWLITRVNALVSPKQD TLSIAILDIYGFEDLSFNSFEQLCINYANENLQYLFNKIVFQEEQEEYIREQMDWREIAF ADNQPCINLISLKPYGILRILDDQCCFPQATDHTFLQKCHYHHGANPLYSKPKMPLPEFT IKHYAGKVTYQVHKFLDKNHDQVRQDVLDLFVHSRTRVVAHLFSSHAAQTAPPRLGKSSS ITRLYKAHTVAAKFQQSLLDLVEKMERCNPLFVRCLKPNHKKEPGLFEPDVMMAQLRYSG VLETVRIRKEGFPVRLPFQVFIDRYRCLVALKLNVPADGDMCVSLLSRLCTVTPDMYRVG ISKLFLKEHLHQLLESMRERVQNRAALTLQRYLRGFFIQRHFRSLRRKIILLQSRARGF
>7UDU_3 regulatory light chain (chains E) VFAMFDQSQIQEFKEAFNMIDQNRDGFIDKEDLHDMLASLGKNPTDEYLDAMMNEAPGPI NFTMFLTMFGEKLNGTDPEDVIRNAFACFDEEATGFIQEDYLRELLTTMGDRFTDEEVDE LYREAPIDKKGNFNYIEFTRILKHGA
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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