9L2N: Cytochalasin D

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.

Method
X-ray diffraction
Resolution
1.7 Å
Organisms
Gallus gallus, Physarum polycephalum
Chains
2
Atoms
4,941
Mol. weight
61.53 kDa
Ligands
CA, CY9, MG, PO4
Released
2 Jul 2025

Explore 9L2N in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 24 helices, 20 β-strands

ElementResiduesLengthSheet
α-helix6-72
β-strand8-1251
β-strand16-2161
β-strand2412
β-strand29-3241
β-strand35-3843
β-strand53-5423
α-helix56-605
α-helix62-643
β-strand65-6843
β-strand71-7224
β-strand75-7624
α-helix79-879
α-helix88-947
α-helix98-1003
β-strand103-10751
α-helix113-12513
β-strand131-13661
α-helix137-1448
β-strand150-15565
β-strand160-16675
β-strand169-17025
α-helix172-1743
β-strand176-17835
α-helix182-19514
α-helix203-21614
α-helix223-23210
β-strand238-24146
β-strand247-25046
α-helix253-26210
α-helix264-2674
α-helix272-2732
α-helix274-28310
α-helix287-2893
α-helix290-2945
β-strand297-30045
α-helix302-3043
α-helix309-32012
β-strand329-33025
α-helix338-34710
α-helix350-3545
β-strand357-35821
α-helix359-3657
α-helix369-3735
Chain B: 9 helices, 8 β-strands
ElementResiduesLengthSheet
α-helix30-323
α-helix34-363
β-strand44-5187
β-strand54-5747
α-helix58-592
α-helix60-623
β-strand65-6738
β-strand71-7887
β-strand88-9587
α-helix101-11717
β-strand123-12867
α-helix134-1374
β-strand146-14838
α-helix152-1543
α-helix1561
β-strand15712
α-helix158-1592

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Actin, alpha skeletal muscleAprotein375Gallus gallusP68139 (AlphaFold model)
Actin-binding protein fragmin PBprotein162Physarum polycephalumQ94707 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>9L2N_1 Actin, alpha skeletal muscle (chains A)
DEDETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQS
KRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREKMT
QIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRLDL
AGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEKSY
ELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVMS
GGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWITKQ
EYDEAGPSIVHRKCF
Sequence of entity 2 (B), FASTA
>9L2N_2 Actin-binding protein fragmin P (chains B)
GPMQKQKEYNIADSAIANLGTELEKKVKLEASQHEDAWKGAGKQVGVEIWRIQQFKVVPV
PKKHHGSFYTGDSYIVLSTYHPKTNPDKLAYDVHFWLGAFTTQDEAGTAAYKTVELDDYL
GGLPVQYREVQGYESERFLSLFPKGGLRILDGGVETGFHHVE

Ligands and cofactors

IDNameFormulaCopies
CACalcium ionCa2
CY9(3S,3aR,4S,6S,6aR,7E,10S,12R,13E,15R,15aR)-3-benzyl-6,12-dihydroxy-4,10,12-trim…C30 H37 N O61
MGMagnesium ionMg1
PO4Phosphate ionO4 P3
ADPAdenosine-5'-diphosphateC10 H15 N5 O10 P21

Water and common crystallization additives (EDO) are not listed.

Primary citation

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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