The structural basis of blebbistatin inhibition and specificity for myosin II. Determined by X-ray diffraction at 2.0 Å resolution. Released 8 Mar 2005.
Explore 1YV3 in 3D Show helices and sheets RCSB PDB PDBe
1YV3 contains 39 α-helices and 31 β-strands across 1 chain. 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 | 3-5 | 3 | |
| α-helix | 10-15 | 6 | |
| α-helix | 17-20 | 4 | |
| α-helix | 22-29 | 8 | |
| β-strand | 34-37 | 4 | 1 |
| β-strand | 48-51 | 4 | 1 |
| β-strand | 52-55 | 4 | 2 |
| β-strand | 59-63 | 5 | 2 |
| β-strand | 69-73 | 5 | 2 |
| α-helix | 74-76 | 3 | |
| β-strand | 78-79 | 2 | 1 |
| α-helix | 80-82 | 3 | |
| α-helix | 83-85 | 3 | |
| β-strand | 90 | 1 | 3 |
| α-helix | 91-93 | 3 | |
| α-helix | 99-111 | 13 | |
| β-strand | 116-119 | 4 | 3 |
| β-strand | 122-126 | 5 | 3 |
| α-helix | 137-143 | 7 | |
| α-helix | 148-150 | 3 | |
| α-helix | 155-169 | 15 | |
| β-strand | 173-178 | 6 | 3 |
| β-strand | 180 | 1 | 4 |
| α-helix | 185-199 | 15 | |
| α-helix | 211-226 | 16 | |
| β-strand | 227-228 | 2 | 5 |
| β-strand | 236-237 | 2 | 5 |
| β-strand | 241-247 | 7 | 3 |
| β-strand | 253-260 | 8 | 3 |
| α-helix | 265-268 | 4 | |
| β-strand | 278 | 1 | 5 |
| α-helix | 279-287 | 9 | |
| α-helix | 292-295 | 4 | |
| α-helix | 301-303 | 3 | |
| α-helix | 320-334 | 15 | |
| α-helix | 338-355 | 18 | |
| β-strand | 360-361 | 2 | 6 |
| β-strand | 367-368 | 2 | 6 |
| α-helix | 373-382 | 10 | |
| α-helix | 386-394 | 9 | |
| β-strand | 397-400 | 4 | 7 |
| β-strand | 403-406 | 4 | 7 |
| α-helix | 411-440 | 30 | |
| β-strand | 448-454 | 7 | 3 |
| α-helix | 455-457 | 3 | |
| β-strand | 458 | 1 | 4 |
| α-helix | 466-483 | 18 | |
| α-helix | 484-488 | 5 | |
| α-helix | 489-496 | 8 | |
| α-helix | 501-503 | 3 | |
| α-helix | 511-518 | 8 | |
| α-helix | 525-533 | 9 | |
| α-helix | 540-551 | 12 | |
| β-strand | 558-559 | 2 | 8 |
| β-strand | 567-572 | 6 | 8 |
| β-strand | 575-580 | 6 | 8 |
| α-helix | 584-589 | 6 | |
| α-helix | 594-601 | 8 | |
| α-helix | 606-613 | 8 | |
| α-helix | 615-618 | 4 | |
| β-strand | 622-623 | 2 | 9 |
| β-strand | 626-627 | 2 | 9 |
| α-helix | 628-629 | 2 | |
| α-helix | 630-646 | 17 | |
| β-strand | 649-656 | 8 | 3 |
| α-helix | 669-679 | 11 | |
| α-helix | 681-690 | 10 | |
| β-strand | 694-697 | 4 | 10 |
| β-strand | 738-739 | 2 | 10 |
| β-strand | 743-746 | 4 | 10 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Myosin II heavy chain | A | protein | 762 | Dictyostelium discoideum | P08799 (AlphaFold model) |
>1YV3_1 Myosin II heavy chain (chains A) GNPIHDRTSDYHKYLKVKQGDSDLFKLTVSDKRYIWYNPDPKERDSYECGEIVSETSDSF TFKTVDGQDRQVKKDDANQRNPIKFDGVEDMSELSYLNEPAVFHNLRVRYNQDLIYTYSG LFLVAVNPFKRIPIYTQEMVDIFKGRRRNEVAPHIFAISDVAYRSMLDDRQNQSLLITGE SGAGKTENTKKVIQYLASVAGRNQANGSGVLEQQILQANPILEAFGNAKTTRNNNSSRFG KFIEIQFNSAGFISGASIQSYLLEKSRVVFQSETERNYHIFYQLLAGATAEEKKALHLAG PESFNYLNQSGCVDIKGVSDSEEFKITRQAMDIVGFSQEEQMSIFKIIAGILHLGNIKFE KGAGEGAVLKDKTALNAASTVFGVNPSVLEKALMEPRILAGRDLVAQHLNVEKSSSSRDA LVKALYGRLFLWLVKKINNVLCQERKAYFIGVLDISGFEIFKVNSFEQLCINYTNEKLQQ FFNHHMFKLEQEEYLKEKINWTFIDFGLDSQATIDLIDGRQPPGILALLDEQSVFPNATD NTLITKLHSHFSKKNAKYEEPRFSKTEFGVTHYAGQVMYEIQDWLEKNKDPLQQDLELCF KDSSDNVVTKLFNDPNIASRAKKGANFITVAAQYKEQLASLMATLETTNPHFVRCIIPNN KQLPAKLEDKVVLDQLRCNGVLEGIRITRKGFPNRIIYADFVKRYYLLAPNVPRDAEDSQ KATDAVLKHLNIDPEQYRFGITKIFFRAGQLARIEEARELPN
| ID | Name | Formula | Copies |
|---|---|---|---|
| BIT | (-)-1-phenyl-1,2,3,4-tetrahydro-4-HYDROXYPYRROLO[2,3-B]-7-methylquinolin-4-one | C18 H16 N2 O2 | 1 |
| ADP | Adenosine-5'-diphosphate | C10 H15 N5 O10 P2 | 1 |
| VO4 | Vanadate ion | O4 V | 1 |
| MG | Magnesium ion | Mg | 2 |
Water and common crystallization additives (EDO) are not listed.
The structural basis of blebbistatin inhibition and specificity for myosin II. Allingham, J.S., Smith, R., Rayment, I. Nat Struct Mol Biol (2005) 12:378-379. DOI 10.1038/nsmb908 · PubMed
Other PDB entries of the same protein (UniProt P08799 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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