M6 delta Insert1. Determined by X-ray diffraction at 2.2 Å resolution. Released 26 Jan 2011.
Explore 2X51 in 3D Show helices and sheets RCSB PDB PDBe
2X51 contains 45 α-helices and 31 β-strands across 2 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 | 7-11 | 5 | 1 |
| β-strand | 15-19 | 5 | 1 |
| β-strand | 28-30 | 3 | 2 |
| β-strand | 42-44 | 3 | 2 |
| α-helix | 45-47 | 3 | |
| β-strand | 49-50 | 2 | 1 |
| β-strand | 61 | 1 | 3 |
| α-helix | 62-64 | 3 | |
| α-helix | 70-82 | 13 | |
| β-strand | 87-90 | 4 | 3 |
| β-strand | 93-97 | 5 | 3 |
| α-helix | 109-114 | 6 | |
| α-helix | 118-119 | 2 | |
| α-helix | 127-141 | 15 | |
| β-strand | 145-150 | 6 | 3 |
| α-helix | 157-172 | 16 | |
| α-helix | 178-193 | 16 | |
| β-strand | 194-195 | 2 | 4 |
| β-strand | 203-204 | 2 | 4 |
| β-strand | 207-214 | 8 | 3 |
| β-strand | 220-228 | 9 | 3 |
| α-helix | 233-235 | 3 | |
| β-strand | 245 | 1 | 4 |
| α-helix | 246-254 | 9 | |
| α-helix | 257-262 | 6 | |
| α-helix | 268-270 | 3 | |
| α-helix | 313-326 | 14 | |
| α-helix | 331-347 | 17 | |
| β-strand | 352-354 | 3 | 5 |
| β-strand | 362-364 | 3 | 5 |
| α-helix | 366-368 | 3 | |
| α-helix | 369-378 | 10 | |
| α-helix | 383-391 | 9 | |
| β-strand | 392-393 | 2 | 6 |
| β-strand | 409-410 | 2 | 6 |
| α-helix | 413-441 | 29 | |
| β-strand | 450-456 | 7 | 3 |
| β-strand | 466 | 1 | 7 |
| α-helix | 468-498 | 31 | |
| α-helix | 512-519 | 8 | |
| α-helix | 525-533 | 9 | |
| α-helix | 540-550 | 11 | |
| β-strand | 557-558 | 2 | 7 |
| α-helix | 560-562 | 3 | |
| β-strand | 576-581 | 6 | 7 |
| β-strand | 584-589 | 6 | 7 |
| α-helix | 593-596 | 4 | |
| α-helix | 600-602 | 3 | |
| α-helix | 603-610 | 8 | |
| α-helix | 615-620 | 6 | |
| α-helix | 643-659 | 17 | |
| β-strand | 662-669 | 8 | 3 |
| α-helix | 682-691 | 10 | |
| α-helix | 694-701 | 8 | |
| β-strand | 707-710 | 4 | 8 |
| α-helix | 711-718 | 8 | |
| α-helix | 719-721 | 3 | |
| α-helix | 724-727 | 4 | |
| α-helix | 731-742 | 12 | |
| β-strand | 749-751 | 3 | 8 |
| β-strand | 755-758 | 4 | 8 |
| α-helix | 762-770 | 9 | |
| α-helix | 774-782 | 9 | |
| α-helix | 785-814 | 30 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 7-20 | 14 | |
| β-strand | 28 | 1 | 9 |
| α-helix | 30-39 | 10 | |
| α-helix | 46-54 | 9 | |
| β-strand | 64 | 1 | 9 |
| α-helix | 66-73 | 8 | |
| α-helix | 82-93 | 12 | |
| β-strand | 100-101 | 2 | 10 |
| α-helix | 103-112 | 10 | |
| α-helix | 119-129 | 11 | |
| β-strand | 137-138 | 2 | 10 |
| α-helix | 139-146 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Myosin-VI | A | protein | 789 | SUS SCROFA | Q29122 (AlphaFold model) |
| Calmodulin | B | protein | 149 | DROSOPHILA MELANOGASTER | P62152 (AlphaFold model) |
>2X51_1 MYOSIN-VI (chains A) MEDGKPVWAPHPTDGFQVGNIVDIGPDSLTIEPLNQKGKTFLALINQVFPAEEDSKKDVE DNCSLMYLNEATLLHNIKVRYSKDRIYTYVANILIAVNPYFDIPKIYSSETIKSYQGKSL GTMPPHVFAIADKAFRDMKVLKLSQSIIVSGESGAGKTENTKFVLRYLTESYGTGQDIDD RIVEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVVGGFVSHYLLEKSRICVQGK EERNYHIFYRLCAGASEDIRERLHLSSPDNFRYLNRGGSLKDPLLDDHGDFIRMCTAMKK IGLDDEEKLDLFRVVAGVLHLGNIDFEEAGSTSGGCNLKNKSTQALEYCAELLGLDQDDL RVSLTTRVMLTTAGGAKGTVIKVPLKVEQANNARDALAKTVYSHLFDHVVNRVNQCFPFE TSSYFIGVLDIAGFEYFEHNSFEQFCINYCNEKLQQFFNERILKEEQELYQKEGLGVNEV HYVDNQDCIDLIEARLVGILDILDEENRLPQPSDQHFTSAVHQKHKDHFRLSIPRKSKLA IHRNIRDDEGFIIRHFAGAVCYETTQFVEKNNDALHMSLESLICESRDKFIRELFESSTN NNKDTKQKAGKLSFISVGNKFKTQLNLLLDKLRSTGASFIRCIKPNLKMTSHHFEGAQIL SQLQCSGMVSVLDLMQGGFPSRASFHELYNMYKKYMPDKLARLDPRLFCKALFKALGLNE IDYKFGLTKVFFRPGKFAEFDQIMKSDPDHLAELVKRVNHWLICSRWKKVQWCSLSVIKL KNKIKYRAE
>2X51_2 CALMODULIN (chains B) MADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADG NGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGFISAAELRHVMTNLGEKLTDE EVDEMIREADIDGDGQVNYEEFVTMMTSK
| ID | Name | Formula | Copies |
|---|---|---|---|
| CA | Calcium ion | Ca | 3 |
Water and common crystallization additives (GOL, SO4) are not listed.
Role of Insert-1 of Myosin Vi in Modulating Nucleotide Affinity. Pylypenko, O., Song, L., Squires, G. et al. J Biol Chem (2011) 286:11716. DOI 10.1074/JBC.M110.200626 · 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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