CryoEM structure of Myosin VI-Actin complex in the ADP state, backbone-averaged with side chains truncated to alanine. Determined by electron microscopy at 5.5 Å resolution. Released 10 Jan 2018.
Explore 6BNW in 3D Show helices and sheets RCSB PDB PDBe
6BNW contains 444 α-helices and 332 β-strands across 14 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 | 55 |
| β-strand | 17-21 | 5 | 55 |
| β-strand | 29-31 | 3 | 55 |
| β-strand | 35-38 | 4 | 56 |
| β-strand | 41 | 1 | 57 |
| β-strand | 53-54 | 2 | 56 |
| α-helix | 57-60 | 4 | |
| β-strand | 65-68 | 4 | 56 |
| β-strand | 71-72 | 2 | 58 |
| β-strand | 75-76 | 2 | 58 |
| α-helix | 79-87 | 9 | |
| α-helix | 88-94 | 7 | |
| α-helix | 98-100 | 3 | |
| β-strand | 103-107 | 5 | 55 |
| α-helix | 115-126 | 12 | |
| β-strand | 131-136 | 6 | 55 |
| α-helix | 137-145 | 9 | |
| β-strand | 149-156 | 8 | 59 |
| β-strand | 159-166 | 8 | 59 |
| β-strand | 169-170 | 2 | 59 |
| α-helix | 172-174 | 3 | |
| β-strand | 176-178 | 3 | 59 |
| α-helix | 183-194 | 12 | |
| α-helix | 203-215 | 13 | |
| α-helix | 223-231 | 9 | |
| β-strand | 238-241 | 4 | 60 |
| β-strand | 247-250 | 4 | 60 |
| α-helix | 252-259 | 8 | |
| α-helix | 272-273 | 2 | |
| α-helix | 274-282 | 9 | |
| α-helix | 287-293 | 7 | |
| β-strand | 297-300 | 4 | 59 |
| α-helix | 302-305 | 4 | |
| α-helix | 311-320 | 10 | |
| α-helix | 322 | 1 | |
| β-strand | 329-330 | 2 | 59 |
| α-helix | 335-337 | 3 | |
| α-helix | 338-348 | 11 | |
| α-helix | 352-355 | 4 | |
| β-strand | 357-358 | 2 | 55 |
| α-helix | 359-365 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 8-11 | 4 | 87 |
| β-strand | 17-21 | 5 | 87 |
| β-strand | 29-31 | 3 | 87 |
| β-strand | 35-38 | 4 | 88 |
| β-strand | 53-54 | 2 | 88 |
| α-helix | 57-60 | 4 | |
| β-strand | 65-68 | 4 | 88 |
| β-strand | 71-72 | 2 | 89 |
| β-strand | 75-76 | 2 | 89 |
| α-helix | 79-87 | 9 | |
| α-helix | 88-94 | 7 | |
| α-helix | 98-100 | 3 | |
| β-strand | 103-107 | 5 | 87 |
| α-helix | 115-126 | 12 | |
| β-strand | 131-136 | 6 | 87 |
| α-helix | 137-145 | 9 | |
| β-strand | 149-156 | 8 | 79 |
| β-strand | 159-166 | 8 | 79 |
| β-strand | 169-170 | 2 | 79 |
| α-helix | 172-174 | 3 | |
| β-strand | 176-178 | 3 | 79 |
| α-helix | 183-194 | 12 | |
| α-helix | 203-215 | 13 | |
| α-helix | 223-231 | 9 | |
| β-strand | 238-241 | 4 | 90 |
| β-strand | 247-250 | 4 | 90 |
| α-helix | 252-259 | 8 | |
| α-helix | 272-273 | 2 | |
| α-helix | 274-282 | 9 | |
| α-helix | 287-293 | 7 | |
| β-strand | 297-300 | 4 | 79 |
| α-helix | 302-305 | 4 | |
| α-helix | 311-320 | 10 | |
| α-helix | 322 | 1 | |
| β-strand | 329-330 | 2 | 79 |
| α-helix | 335-337 | 3 | |
| α-helix | 338-348 | 11 | |
| α-helix | 352-355 | 4 | |
| β-strand | 357-358 | 2 | 87 |
| α-helix | 359-365 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 7-11 | 5 | 1 |
| β-strand | 15-23 | 9 | 1 |
| β-strand | 29-33 | 5 | 1 |
| β-strand | 41-43 | 3 | 1 |
| α-helix | 45-47 | 3 | |
| β-strand | 49-50 | 2 | 1 |
| β-strand | 61 | 1 | 2 |
| α-helix | 62-64 | 3 | |
| α-helix | 70-82 | 13 | |
| β-strand | 87-90 | 4 | 2 |
| β-strand | 93-97 | 5 | 2 |
| α-helix | 102-103 | 2 | |
| α-helix | 109-115 | 7 | |
| α-helix | 118-119 | 2 | |
| β-strand | 120 | 1 | 3 |
| β-strand | 123 | 1 | 3 |
| α-helix | 128-140 | 13 | |
| β-strand | 145-150 | 6 | 2 |
| α-helix | 159-168 | 10 | |
| α-helix | 180-193 | 14 | |
| β-strand | 194-195 | 2 | 4 |
| β-strand | 203-204 | 2 | 4 |
| β-strand | 207-213 | 7 | 2 |
| β-strand | 222-228 | 7 | 2 |
| α-helix | 233-236 | 4 | |
| α-helix | 248-252 | 5 | |
| α-helix | 257-260 | 4 | |
| α-helix | 268-270 | 3 | |
| β-strand | 282 | 1 | 5 |
| α-helix | 285-290 | 6 | |
| α-helix | 293-295 | 3 | |
| α-helix | 298-303 | 6 | |
| α-helix | 305 | 1 | |
| β-strand | 306 | 1 | 5 |
| α-helix | 307 | 1 | |
| α-helix | 313-326 | 14 | |
| α-helix | 331-347 | 17 | |
| β-strand | 352-355 | 4 | 6 |
| β-strand | 361-364 | 4 | 6 |
| α-helix | 366-368 | 3 | |
| α-helix | 370-379 | 10 | |
| α-helix | 383-390 | 8 | |
| β-strand | 392-396 | 5 | 7 |
| β-strand | 406-410 | 5 | 7 |
| α-helix | 411-412 | 2 | |
| α-helix | 413-440 | 28 | |
| β-strand | 451-456 | 6 | 2 |
| α-helix | 468-484 | 17 | |
| α-helix | 485-489 | 5 | |
| α-helix | 490-496 | 7 | |
| α-helix | 512-518 | 7 | |
| α-helix | 526-534 | 9 | |
| α-helix | 540-550 | 11 | |
| β-strand | 557-558 | 2 | 8 |
| α-helix | 560-562 | 3 | |
| α-helix | 566-569 | 4 | |
| α-helix | 573-575 | 3 | |
| β-strand | 576-581 | 6 | 8 |
| β-strand | 584-589 | 6 | 8 |
| α-helix | 593-596 | 4 | |
| α-helix | 603-609 | 7 | |
| α-helix | 615-620 | 6 | |
| α-helix | 644-659 | 16 | |
| β-strand | 662-669 | 8 | 2 |
| α-helix | 684-690 | 7 | |
| α-helix | 694-700 | 7 | |
| β-strand | 707-710 | 4 | 9 |
| α-helix | 711-718 | 8 | |
| α-helix | 719-721 | 3 | |
| α-helix | 726-728 | 3 | |
| α-helix | 731-742 | 12 | |
| β-strand | 749-751 | 3 | 9 |
| β-strand | 755-758 | 4 | 9 |
| α-helix | 763-770 | 8 | |
| α-helix | 774-790 | 17 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 7-11 | 5 | 10 |
| β-strand | 15-23 | 9 | 10 |
| β-strand | 29-33 | 5 | 10 |
| β-strand | 41-43 | 3 | 10 |
| α-helix | 45-47 | 3 | |
| β-strand | 49-50 | 2 | 10 |
| β-strand | 61 | 1 | 11 |
| α-helix | 62-64 | 3 | |
| α-helix | 70-82 | 13 | |
| β-strand | 87-90 | 4 | 11 |
| β-strand | 93-97 | 5 | 11 |
| α-helix | 102-103 | 2 | |
| α-helix | 109-115 | 7 | |
| α-helix | 118-119 | 2 | |
| β-strand | 120 | 1 | 12 |
| β-strand | 123 | 1 | 12 |
| α-helix | 128-140 | 13 | |
| β-strand | 145-150 | 6 | 11 |
| α-helix | 159-168 | 10 | |
| α-helix | 181-193 | 13 | |
| β-strand | 194-195 | 2 | 13 |
| β-strand | 203-204 | 2 | 13 |
| β-strand | 207-213 | 7 | 11 |
| β-strand | 222-228 | 7 | 11 |
| α-helix | 233-236 | 4 | |
| α-helix | 248-252 | 5 | |
| α-helix | 257-260 | 4 | |
| α-helix | 268-270 | 3 | |
| β-strand | 282 | 1 | 14 |
| α-helix | 285-290 | 6 | |
| α-helix | 293-295 | 3 | |
| α-helix | 298-303 | 6 | |
| α-helix | 305 | 1 | |
| β-strand | 306 | 1 | 14 |
| α-helix | 307 | 1 | |
| α-helix | 313-326 | 14 | |
| α-helix | 331-347 | 17 | |
| β-strand | 352-355 | 4 | 15 |
| β-strand | 361-364 | 4 | 15 |
| α-helix | 366-368 | 3 | |
| α-helix | 370-379 | 10 | |
| α-helix | 383-390 | 8 | |
| β-strand | 392-396 | 5 | 16 |
| β-strand | 406-410 | 5 | 16 |
| α-helix | 411-412 | 2 | |
| α-helix | 413-440 | 28 | |
| β-strand | 451-456 | 6 | 11 |
| α-helix | 468-484 | 17 | |
| α-helix | 485-489 | 5 | |
| α-helix | 490-496 | 7 | |
| α-helix | 512-518 | 7 | |
| α-helix | 526-534 | 9 | |
| α-helix | 540-550 | 11 | |
| β-strand | 557-558 | 2 | 17 |
| α-helix | 560-562 | 3 | |
| α-helix | 566-569 | 4 | |
| α-helix | 573-575 | 3 | |
| β-strand | 576-581 | 6 | 17 |
| β-strand | 584-589 | 6 | 17 |
| α-helix | 593-596 | 4 | |
| α-helix | 603-609 | 7 | |
| α-helix | 615-620 | 6 | |
| α-helix | 644-659 | 16 | |
| β-strand | 662-669 | 8 | 11 |
| α-helix | 684-690 | 7 | |
| α-helix | 694-700 | 7 | |
| β-strand | 707-710 | 4 | 18 |
| α-helix | 711-718 | 8 | |
| α-helix | 719-721 | 3 | |
| α-helix | 726-728 | 3 | |
| α-helix | 731-742 | 12 | |
| β-strand | 749-751 | 3 | 18 |
| β-strand | 755-758 | 4 | 18 |
| α-helix | 763-770 | 8 | |
| α-helix | 774-790 | 17 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Unconventional myosin-VI | I, J, K, L, M, N | protein | 816 | Sus scrofa | Q29122 (AlphaFold model) |
| Actin, alpha skeletal muscle | A, B, C, D, E, F, G, H | protein | 373 | Oryctolagus cuniculus | P68135 (AlphaFold model) |
>6BNW_1 Unconventional myosin-VI (chains I, J, K, L, M, N) EDGKPVWAPHPTDGFQVGNIVDIGPDSLTIEPLNQKGKTFLALINQVFPAEEDSKKDVED NCSLMYLNEATLLHNIKVRYSKDRIYTYVANILIAVNPYFDIPKIYSSETIKSYQGKSLG TMPPHVFAIADKAFRDMKVLKLSQSIIVSGESGAGKTENTKFVLRYLTESYGTGQDIDDR IVEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVVGGFVSHYLLEKSRICVQGKE ERNYHIFYRLCAGASEDIRERLHLSSPDNFRYLNRGCTRYFANKETDKQILQNRKSPEYL KAGSLKDPLLDDHGDFIRMCTAMKKIGLDDEEKLDLFRVVAGVLHLGNIDFEEAGSTSGG CNLKNKSTQALEYCAELLGLDQDDLRVSLTTRVMLTTAGGAKGTVIKVPLKVEQANNARD ALAKTVYSHLFDHVVNRVNQCFPFETSSYFIGVLDIAGFEYFEHNSFEQFCINYCNEKLQ QFFNERILKEEQELYQKEGLGVNEVHYVDNQDCIDLIEARLVGILDILDEENRLPQPSDQ HFTSAVHQKHKDHFRLSIPRKSKLAIHRNIRDDEGFIIRHFAGAVCYETTQFVEKNNDAL HMSLESLICESRDKFIRELFESSTNNNKDTKQKAGKLSFISVGNKFKTQLNLLLDKLRST GASFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPSRASFHELYNMYKKY MPDKLARLDPRLFCKALFKALGLNEIDYKFGLTKVFFRPGKFAEFDQIMKSDPDHLAELV KRVNHWLICSRWKKVQWCSLSVIKLKNKIKYRAEAC
>6BNW_2 Actin, alpha skeletal muscle (chains A, B, C, D, E, F, G, H) MCDEDETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEA QSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREK MTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRL DLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEK SYELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNV MSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWIT KQEYDEAGPSIVH
Cryo-EM structures reveal specialization at the myosin VI-actin interface and a mechanism of force sensitivity. Gurel, P.S., Kim, L.Y., Ruijgrok, P.V. et al. Elife (2017) 6. DOI 10.7554/eLife.31125 · PubMed
Other PDB entries of the same protein (UniProt Q29122 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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