Structure of Scallop myosin S1 reveals a novel nucleotide conformation. Determined by X-ray diffraction at 3.1 Å resolution. Released 22 Jun 2004.
Explore 1S5G in 3D Show helices and sheets RCSB PDB PDBe
1S5G contains 51 α-helices and 40 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 |
|---|---|---|---|
| α-helix | 8-12 | 5 | |
| β-strand | 33-38 | 6 | 1 |
| β-strand | 42-51 | 10 | 1 |
| β-strand | 55-59 | 5 | 1 |
| β-strand | 67-70 | 4 | 1 |
| α-helix | 71-73 | 3 | |
| β-strand | 75-76 | 2 | 1 |
| α-helix | 80-82 | 3 | |
| β-strand | 87 | 1 | 2 |
| α-helix | 96-108 | 13 | |
| β-strand | 113-116 | 4 | 2 |
| β-strand | 119-123 | 5 | 2 |
| α-helix | 134-140 | 7 | |
| α-helix | 152-166 | 15 | |
| β-strand | 170-175 | 6 | 3 |
| α-helix | 182-194 | 13 | |
| α-helix | 215-230 | 16 | |
| β-strand | 231-232 | 2 | 4 |
| β-strand | 240-241 | 2 | 4 |
| β-strand | 244-251 | 8 | 3 |
| β-strand | 257-261 | 5 | 3 |
| β-strand | 264-265 | 2 | 3 |
| α-helix | 269-272 | 4 | |
| α-helix | 283-288 | 6 | |
| α-helix | 294-300 | 7 | |
| α-helix | 306-308 | 3 | |
| β-strand | 319 | 1 | 5 |
| β-strand | 322 | 1 | 5 |
| α-helix | 326-338 | 13 | |
| α-helix | 342-357 | 16 | |
| α-helix | 358-360 | 3 | |
| β-strand | 363-364 | 2 | 6 |
| β-strand | 373-374 | 2 | 6 |
| α-helix | 378-387 | 10 | |
| α-helix | 391-399 | 9 | |
| β-strand | 402 | 1 | 7 |
| β-strand | 405 | 1 | 8 |
| β-strand | 408 | 1 | 8 |
| β-strand | 411 | 1 | 7 |
| α-helix | 416-446 | 31 | |
| β-strand | 454-460 | 7 | 3 |
| β-strand | 470 | 1 | 9 |
| α-helix | 472-502 | 31 | |
| α-helix | 515-524 | 10 | |
| α-helix | 529-535 | 7 | |
| α-helix | 544-555 | 12 | |
| β-strand | 562-563 | 2 | 9 |
| α-helix | 564-567 | 4 | |
| β-strand | 578-582 | 5 | 9 |
| β-strand | 585-589 | 5 | 9 |
| α-helix | 594-598 | 5 | |
| α-helix | 604-611 | 8 | |
| α-helix | 616-621 | 6 | |
| α-helix | 645-660 | 16 | |
| β-strand | 664 | 1 | 3 |
| β-strand | 667-669 | 3 | 3 |
| β-strand | 670-671 | 2 | 2 |
| α-helix | 684-694 | 11 | |
| α-helix | 696-704 | 9 | |
| β-strand | 710-711 | 2 | 10 |
| α-helix | 713-720 | 8 | |
| α-helix | 725-727 | 3 | |
| α-helix | 735-745 | 11 | |
| β-strand | 753-755 | 3 | 10 |
| β-strand | 760-762 | 3 | 10 |
| α-helix | 766-822 | 57 | |
| α-helix | 825-832 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 15-17 | 3 | |
| α-helix | 22-24 | 3 | |
| α-helix | 39-45 | 7 | |
| α-helix | 54-57 | 4 | |
| α-helix | 86-92 | 7 | |
| α-helix | 93-96 | 4 | |
| β-strand | 104-105 | 2 | 11 |
| α-helix | 106-115 | 10 | |
| α-helix | 122-128 | 7 | |
| β-strand | 134-135 | 2 | 11 |
| β-strand | 138-139 | 2 | 11 |
| α-helix | 141-149 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 9-20 | 12 | |
| β-strand | 29 | 1 | 12 |
| α-helix | 30-38 | 9 | |
| α-helix | 46-50 | 5 | |
| β-strand | 62 | 1 | 12 |
| α-helix | 65-76 | 12 | |
| α-helix | 83-91 | 9 | |
| β-strand | 100-102 | 3 | 13 |
| α-helix | 103-112 | 10 | |
| α-helix | 119-129 | 11 | |
| β-strand | 138-140 | 3 | 13 |
| α-helix | 141-150 | 10 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Myosin heavy chain, striated muscle | A | protein | 840 | Argopecten irradians | P24733 (AlphaFold model) |
| Myosin regulatory light chain, striated adductor muscle | Y | protein | 156 | Argopecten irradians | P13543 (AlphaFold model) |
| Myosin essential light chain, striated adductor muscle | Z | protein | 156 | Argopecten irradians | P07291 (AlphaFold model) |
>1S5G_1 Myosin heavy chain, striated muscle (chains A) MNIDFSDPDFQYLAVDRKKLMKEQTAAFDGKKNCWVPDEKEGFASAEIQSSKGDEITVKI VADSSTRTVKKDDIQSMNPPKFEKLEDMANMTYLNEASVLYNLRSRYTSGLIYTYSGLFC IAVNPYRRLPIYTDSVIAKYRGKRKTEIPPHLFSVADNAYQNMVTDRENQSCLITGESGA GKTENTKKVIMYLAKVACAVKKKDEEASDKKEGSLEDQIIQANPVLEAYGNAKTTRNNNS SRFGKFIRIHFGPTGKIAGADIETYLLEKSRVTYQQSAERNYHIFYQICSNAIPELNDVM LVTPDSGLYSFINQGCLTVDNIDDVEEFKLCDEAFDILGFTKEEKQSMFKCTASILHMGE MKFKQRPREEQAESDGTAEAEKVAFLCGINAGDLLKALLKPKVKVGTEMVTKGQNMNQVV NSVGALAKSLYDRMFNWLVRRVNKTLDTKAKRNYYIGVLDIAGFEIFDFNSFEQLCINYT NERLQQFFNHHMFILEQEEYKKEGIAWEFIDFGMDLQMCIDLIEKPMGILSILEEECMFP KADDKSFQDKLYQNHMGKNRMFTKPGKPTRPNQGPAHFELHHYAGNVPYSITGWLEKNKD PINENVVALLGASKEPLVAELFKAPEEPAGGGKKKKGKSSAFQTISAVHRESLNKLMKNL YSTHPHFVRCIIPNELKQPGLVDAELVLHQLQCNGVLEGIRICRKGFPSRLIYSEFKQRY SILAPNAIPQGFVDGKTVSEKILAGLQMDPAEYRLGTTKVFFKAGVLGNLEEMRDERLSK IISMFQAHIRGYLIRKAYKKLQDQRIGLSVIQRNIRKWLVLRNWQWWKLYSKVKPLLSIA
>1S5G_2 Myosin regulatory light chain, striated adductor muscle (chains Y) ADKAASGVLTKLPQKQIQEMKEAFSMIDVDRDGFVSKEDIKAISEQLGRAPDDKELTAML KEAPGPLNFTMFLSIFSDKLSGTDSEETIRNAFAMFDEQETKKLNIEYIKDLLENMGDNF NKDEMRMTFKEAPVEGGKFDYVKFTAMIKGSGEEEA
>1S5G_3 Myosin essential light chain, striated adductor muscle (chains Z) PKLSQDEIDDLKDVFELFDFWDGRDGAVDAFKLGDVCRCLGINPRNEDVFAVGGTHKMGE KSLPFEEFLPAYEGLMDCEQGTFADYMEAFKTFDREGQGFISGAELRHVLTALGERLSDE DVDEIIKLTDLQEDLEGNVKYEDFVKKVMAGPYPDK
Water and common crystallization additives (SO4) are not listed.
Myosin subfragment 1 structures reveal a partially bound nucleotide and a complex salt bridge that helps couple nucleotide and actin binding. Risal, D., Gourinath, S., Himmel, D.M. et al. Proc Natl Acad Sci U S A (2004) 101:8930-8935. DOI 10.1073/pnas.0403002101 · PubMed
Other PDB entries of the same protein (UniProt P24733 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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