Crystal structure of Cytochalasin D bound to a filamentous conformation actin. Determined by X-ray diffraction at 1.7 Å resolution. Released 2 Jul 2025.
Explore 9L2N in 3D Show helices and sheets RCSB PDB PDBe
9L2N contains 33 α-helices and 28 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 |
|---|---|---|---|
| α-helix | 6-7 | 2 | |
| β-strand | 8-12 | 5 | 1 |
| β-strand | 16-21 | 6 | 1 |
| β-strand | 24 | 1 | 2 |
| β-strand | 29-32 | 4 | 1 |
| β-strand | 35-38 | 4 | 3 |
| β-strand | 53-54 | 2 | 3 |
| α-helix | 56-60 | 5 | |
| α-helix | 62-64 | 3 | |
| β-strand | 65-68 | 4 | 3 |
| β-strand | 71-72 | 2 | 4 |
| β-strand | 75-76 | 2 | 4 |
| α-helix | 79-87 | 9 | |
| α-helix | 88-94 | 7 | |
| α-helix | 98-100 | 3 | |
| β-strand | 103-107 | 5 | 1 |
| α-helix | 113-125 | 13 | |
| β-strand | 131-136 | 6 | 1 |
| α-helix | 137-144 | 8 | |
| β-strand | 150-155 | 6 | 5 |
| β-strand | 160-166 | 7 | 5 |
| β-strand | 169-170 | 2 | 5 |
| α-helix | 172-174 | 3 | |
| β-strand | 176-178 | 3 | 5 |
| α-helix | 182-195 | 14 | |
| α-helix | 203-216 | 14 | |
| α-helix | 223-232 | 10 | |
| β-strand | 238-241 | 4 | 6 |
| β-strand | 247-250 | 4 | 6 |
| α-helix | 253-262 | 10 | |
| α-helix | 264-267 | 4 | |
| α-helix | 272-273 | 2 | |
| α-helix | 274-283 | 10 | |
| α-helix | 287-289 | 3 | |
| α-helix | 290-294 | 5 | |
| β-strand | 297-300 | 4 | 5 |
| α-helix | 302-304 | 3 | |
| α-helix | 309-320 | 12 | |
| β-strand | 329-330 | 2 | 5 |
| α-helix | 338-347 | 10 | |
| α-helix | 350-354 | 5 | |
| β-strand | 357-358 | 2 | 1 |
| α-helix | 359-365 | 7 | |
| α-helix | 369-373 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 30-32 | 3 | |
| α-helix | 34-36 | 3 | |
| β-strand | 44-51 | 8 | 7 |
| β-strand | 54-57 | 4 | 7 |
| α-helix | 58-59 | 2 | |
| α-helix | 60-62 | 3 | |
| β-strand | 65-67 | 3 | 8 |
| β-strand | 71-78 | 8 | 7 |
| β-strand | 88-95 | 8 | 7 |
| α-helix | 101-117 | 17 | |
| β-strand | 123-128 | 6 | 7 |
| α-helix | 134-137 | 4 | |
| β-strand | 146-148 | 3 | 8 |
| α-helix | 152-154 | 3 | |
| α-helix | 156 | 1 | |
| β-strand | 157 | 1 | 2 |
| α-helix | 158-159 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Actin, alpha skeletal muscle | A | protein | 375 | Gallus gallus | P68139 (AlphaFold model) |
| Actin-binding protein fragmin P | B | protein | 162 | Physarum polycephalum | Q94707 (AlphaFold model) |
>9L2N_1 Actin, alpha skeletal muscle (chains A) DEDETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQS KRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREKMT QIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRLDL AGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEKSY ELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVMS GGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWITKQ EYDEAGPSIVHRKCF
>9L2N_2 Actin-binding protein fragmin P (chains B) GPMQKQKEYNIADSAIANLGTELEKKVKLEASQHEDAWKGAGKQVGVEIWRIQQFKVVPV PKKHHGSFYTGDSYIVLSTYHPKTNPDKLAYDVHFWLGAFTTQDEAGTAAYKTVELDDYL GGLPVQYREVQGYESERFLSLFPKGGLRILDGGVETGFHHVE
| ID | Name | Formula | Copies |
|---|---|---|---|
| CA | Calcium ion | Ca | 2 |
| CY9 | (3S,3aR,4S,6S,6aR,7E,10S,12R,13E,15R,15aR)-3-benzyl-6,12-dihydroxy-4,10,12-trim… | C30 H37 N O6 | 1 |
| MG | Magnesium ion | Mg | 1 |
| PO4 | Phosphate ion | O4 P | 3 |
| ADP | Adenosine-5'-diphosphate | C10 H15 N5 O10 P2 | 1 |
Water and common crystallization additives (EDO) are not listed.
Microscopic and structural observations of actin filament capping and severing by cytochalasin D. Mitani, T., Takeda, S., Oda, T. et al. Proc Natl Acad Sci U S A (2025) 122:e2502164122-e2502164122. DOI 10.1073/pnas.2502164122 · PubMed
Other PDB entries of the same protein (UniProt P68139 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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