Cryo-EM structure of the actomyosin-V complex in the rigor state (central 1er, class 2). Determined by electron microscopy at 3.5 Å resolution. Released 22 Dec 2021.
Explore 7PLW in 3D Show helices and sheets RCSB PDB PDBe
7PLW contains 68 α-helices and 53 β-strands across 3 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 | 11-16 | 6 | 4 |
| β-strand | 22-27 | 6 | 4 |
| β-strand | 37-42 | 6 | 4 |
| β-strand | 45-51 | 7 | 4 |
| α-helix | 60-61 | 2 | |
| β-strand | 62 | 1 | 4 |
| β-strand | 73 | 1 | 5 |
| α-helix | 82-95 | 14 | |
| β-strand | 100-103 | 4 | 5 |
| β-strand | 106-110 | 5 | 5 |
| α-helix | 121-127 | 7 | |
| α-helix | 132-134 | 3 | |
| α-helix | 140-152 | 13 | |
| β-strand | 157-163 | 7 | 5 |
| α-helix | 165-167 | 3 | |
| α-helix | 169-183 | 15 | |
| α-helix | 192-207 | 16 | |
| β-strand | 208-209 | 2 | 6 |
| β-strand | 217-218 | 2 | 6 |
| β-strand | 221-228 | 8 | 5 |
| β-strand | 234-242 | 9 | 5 |
| α-helix | 246-249 | 4 | |
| α-helix | 260-267 | 8 | |
| α-helix | 272-277 | 6 | |
| α-helix | 286-289 | 4 | |
| β-strand | 296 | 1 | 7 |
| β-strand | 299 | 1 | 7 |
| α-helix | 301-315 | 15 | |
| α-helix | 319-337 | 19 | |
| β-strand | 341-344 | 4 | 8 |
| β-strand | 347-349 | 3 | 8 |
| α-helix | 355-364 | 10 | |
| α-helix | 368-375 | 8 | |
| β-strand | 377-382 | 6 | 9 |
| β-strand | 385-390 | 6 | 9 |
| α-helix | 393-423 | 31 | |
| β-strand | 431-439 | 9 | 5 |
| α-helix | 440-441 | 2 | |
| β-strand | 447 | 1 | 10 |
| α-helix | 449-479 | 31 | |
| α-helix | 484-486 | 3 | |
| α-helix | 493-500 | 8 | |
| α-helix | 507-514 | 8 | |
| α-helix | 520-531 | 12 | |
| β-strand | 538-539 | 2 | 10 |
| β-strand | 547-551 | 5 | 10 |
| β-strand | 556-560 | 5 | 10 |
| α-helix | 565-568 | 4 | |
| α-helix | 574-581 | 8 | |
| α-helix | 588-593 | 6 | |
| α-helix | 630-633 | 4 | |
| α-helix | 636-651 | 16 | |
| β-strand | 655-662 | 8 | 5 |
| α-helix | 675-684 | 10 | |
| α-helix | 687-695 | 9 | |
| β-strand | 700-703 | 4 | 11 |
| α-helix | 704-711 | 8 | |
| α-helix | 712-714 | 3 | |
| α-helix | 724-735 | 12 | |
| β-strand | 742-744 | 3 | 11 |
| β-strand | 748-751 | 4 | 11 |
| α-helix | 755-791 | 37 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 6-18 | 13 | |
| β-strand | 26-28 | 3 | 1 |
| α-helix | 29-38 | 10 | |
| α-helix | 45-52 | 8 | |
| α-helix | 57-62 | 6 | |
| β-strand | 64-66 | 3 | 1 |
| α-helix | 67-78 | 12 | |
| α-helix | 87-94 | 8 | |
| β-strand | 105 | 1 | 2 |
| α-helix | 106-115 | 10 | |
| α-helix | 119-121 | 3 | |
| α-helix | 122-129 | 8 | |
| β-strand | 133 | 1 | 3 |
| β-strand | 138 | 1 | 2 |
| β-strand | 139 | 1 | 3 |
| α-helix | 141-149 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 8-11 | 4 | 12 |
| β-strand | 16-21 | 6 | 12 |
| β-strand | 29-32 | 4 | 12 |
| β-strand | 35-38 | 4 | 13 |
| β-strand | 53-54 | 2 | 13 |
| α-helix | 56-60 | 5 | |
| α-helix | 62-64 | 3 | |
| β-strand | 65-68 | 4 | 13 |
| β-strand | 71-72 | 2 | 14 |
| β-strand | 75-76 | 2 | 14 |
| α-helix | 79-87 | 9 | |
| α-helix | 88-94 | 7 | |
| α-helix | 98-100 | 3 | |
| β-strand | 103-107 | 5 | 12 |
| α-helix | 113-121 | 9 | |
| α-helix | 122-127 | 6 | |
| β-strand | 131-136 | 6 | 12 |
| α-helix | 137-144 | 8 | |
| β-strand | 150-155 | 6 | 15 |
| β-strand | 160-166 | 7 | 15 |
| β-strand | 169-170 | 2 | 15 |
| α-helix | 172-174 | 3 | |
| β-strand | 176-178 | 3 | 15 |
| α-helix | 182-195 | 14 | |
| α-helix | 203-216 | 14 | |
| α-helix | 223-232 | 10 | |
| β-strand | 238-241 | 4 | 16 |
| β-strand | 247-250 | 4 | 16 |
| α-helix | 252-259 | 8 | |
| α-helix | 264-266 | 3 | |
| α-helix | 274-284 | 11 | |
| α-helix | 290-295 | 6 | |
| β-strand | 297-300 | 4 | 15 |
| α-helix | 302-305 | 4 | |
| α-helix | 309-318 | 10 | |
| β-strand | 330 | 1 | 15 |
| α-helix | 333-337 | 5 | |
| α-helix | 338-348 | 11 | |
| α-helix | 350-354 | 5 | |
| β-strand | 357-358 | 2 | 12 |
| α-helix | 359-365 | 7 | |
| α-helix | 366-368 | 3 | |
| α-helix | 369-373 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Myosin light chain 6B | B | protein | 151 | Homo sapiens | P14649 (AlphaFold model) |
| Unconventional myosin-Va | A | protein | 792 | Gallus gallus | Q02440 (AlphaFold model) |
| Actin, alpha skeletal muscle | C | protein | 377 | Oryctolagus cuniculus | P68135 (AlphaFold model) |
| Phalloidin | H | protein | 7 | synthetic construct |
>7PLW_1 Myosin light chain 6B (chains B) MIEFNKDQLEEFKEAFELFDRVGDGKILYSQCGDVMRALGQNPTNAEVLKVLGNPKSDEL KSRRVDFETFLPMLQAVAKNRGQGTYEDYLEGFRVFDKEGNGKVMGAELRHVLTTLGEKM TEEEVETVLAGHEDSNGCINYEAFLKHILSV
>7PLW_2 Unconventional myosin-Va (chains A) MAASELYTKYARVWIPDPEEVWKSAELLKDYKPGDKVLQLRLEEGKDLEYCLDPKTKELP PLRNPDILVGENDLTALSYLHEPAVLHNLKVRFIDSKLIYTYCGIVLVAINPYEQLPIYG EDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSGESGAGKTVSAKYAMRYF ATVSGSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMR TYLLEKSRVVFQAEEERNYHIFYQLCASAALPEFKTLRLGNANYFHYTKQGGSPVIDGID DAKEMVNTRQACTLLGISDSYQMGIFRILAGILHLGNVEFASRDSDSCAIPPKHDPLTIF CDLMGVDYEEMAHWLCHRKLATATETYIKPISKLHAINARDALAKHIYANLFNWIVDHVN KALHSTVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKE QIPWTLIDFYDNQPCINLIEAKMGVLDLLDEECKMPKGSDDTWAQKLYNTHLNKCALFEK PRLSNKAFIIKHFADKVEYQCEGFLEKNKDTVYEEQIKVLKSSKKFKLLPELFQDEEKAI SPTSATPSGRVPLSRTPVKPAKARPGQTSKEHKKTVGHQFRNSLHLLMETLNATTPHYVR CIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMKQKDV LSDRKQTCKNVLEKLILDKDKYQFGKTKIFFRAGQVAYLEKIRADKLRAACIRIQKTIRG WLMRKKYMRMRR
>7PLW_3 Actin, alpha skeletal muscle (chains C) MCDEDETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEA QSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREK MTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRL DLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEK SYELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNV MSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWIT KQEYDEAGPSIVHRKCF
>7PLW_4 Phalloidin (chains H) WXATCPA
High-resolution structures of the actomyosin-V complex in three nucleotide states provide insights into the force generation mechanism. Pospich, S., Sweeney, H.L., Houdusse, A. et al. Elife (2021) 10. DOI 10.7554/eLife.73724 · PubMed
Other PDB entries of the same protein (UniProt P14649 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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