Insights into the Importance of Hydrogen Bonding in the Gamma-Phosphate Binding Pocket of Myosin: Structural and Functional Studies of Ser236. Determined by X-ray diffraction at 2.01 Å resolution. Released 26 May 2010.
Explore 3MYH in 3D Show helices and sheets RCSB PDB PDBe
3MYH contains 36 α-helices and 32 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 | 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 | 210-226 | 17 | |
| 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 | 266-269 | 4 | |
| β-strand | 278 | 1 | 5 |
| α-helix | 279-287 | 9 | |
| α-helix | 290-295 | 6 | |
| α-helix | 301-303 | 3 | |
| α-helix | 320-334 | 15 | |
| α-helix | 338-356 | 19 | |
| 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 | 411-441 | 31 | |
| β-strand | 448-454 | 7 | 3 |
| α-helix | 455-457 | 3 | |
| β-strand | 458 | 1 | 4 |
| β-strand | 464 | 1 | 8 |
| α-helix | 466-483 | 18 | |
| α-helix | 484-488 | 5 | |
| α-helix | 489-497 | 9 | |
| 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 | 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-2 heavy chain | X | protein | 762 | Dictyostelium discoideum | P08799 (AlphaFold model) |
>3MYH_1 Myosin-2 heavy chain (chains X) GNPIHDRTSDYHKYLKVKQGDSDLFKLTVSDKRYIWYNPDPKERDSYECGEIVSETSDSF TFKTVDGQDRQVKKDDANQRNPIKFDGVEDMSELSYLNEPAVFHNLRVRYNQDLIYTYSG LFLVAVNPFKRIPIYTQEMVDIFKGRRRNEVAPHIFAISDVAYRSMLDDRQNQSLLITGE SGAGKTENTKKVIQYLASVAGRNQANGSGVLEQQILQANPILEAFGNAKTTRNNNASRFG 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 | 1 |
Insights into the importance of hydrogen bonding in the gamma-phosphate binding pocket of myosin: structural and functional studies of serine 236. Frye, J.J., Klenchin, V.A., Bagshaw, C.R. et al. Biochemistry (2010) 49:4897-4907. DOI 10.1021/bi1001344 · 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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