Crystal structure of actin capping protein in complex with V-1 (space group P62). Determined by X-ray diffraction at 2.8 Å resolution. Released 3 Mar 2021.
Explore 7DSA in 3D Show helices and sheets RCSB PDB PDBe
7DSA contains 28 α-helices and 22 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 | 12-22 | 11 | |
| α-helix | 24-25 | 2 | |
| α-helix | 29-40 | 12 | |
| α-helix | 43-49 | 7 | |
| α-helix | 51-60 | 10 | |
| β-strand | 63-65 | 3 | 1 |
| β-strand | 74-76 | 3 | 1 |
| β-strand | 81 | 1 | 2 |
| β-strand | 86-89 | 4 | 2 |
| β-strand | 94-99 | 6 | 2 |
| β-strand | 104-110 | 7 | 2 |
| α-helix | 118-135 | 18 | |
| β-strand | 139-148 | 10 | 3 |
| β-strand | 151-164 | 14 | 3 |
| α-helix | 165-167 | 3 | |
| β-strand | 169-182 | 14 | 3 |
| β-strand | 185-198 | 14 | 3 |
| β-strand | 203-217 | 15 | 3 |
| α-helix | 223-249 | 27 | |
| α-helix | 250-254 | 5 | |
| α-helix | 255-258 | 4 | |
| α-helix | 271-273 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 3-13 | 11 | |
| α-helix | 21-31 | 11 | |
| α-helix | 33-35 | 3 | |
| α-helix | 36-40 | 5 | |
| α-helix | 46-47 | 2 | |
| β-strand | 48-51 | 4 | 4 |
| β-strand | 58-61 | 4 | 4 |
| β-strand | 66-67 | 2 | 5 |
| β-strand | 70-71 | 2 | 5 |
| β-strand | 72 | 1 | 6 |
| β-strand | 79 | 1 | 6 |
| α-helix | 91-112 | 22 | |
| β-strand | 116-123 | 8 | 3 |
| β-strand | 127-137 | 11 | 3 |
| β-strand | 144-159 | 16 | 3 |
| β-strand | 164-181 | 18 | 3 |
| β-strand | 185-202 | 18 | 3 |
| α-helix | 209-230 | 22 | |
| α-helix | 231-235 | 5 | |
| α-helix | 236-243 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 3-12 | 10 | |
| α-helix | 15-23 | 9 | |
| α-helix | 30-32 | 3 | |
| α-helix | 38-44 | 7 | |
| α-helix | 48-56 | 9 | |
| α-helix | 71-78 | 8 | |
| α-helix | 81-89 | 9 | |
| α-helix | 111-116 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| F-actin-capping protein subunit alpha-1 | A | protein | 286 | Gallus gallus | P13127 (AlphaFold model) |
| F-actin-capping protein subunit beta isoforms 1 | B | protein | 244 | Gallus gallus | P14315 (AlphaFold model) |
| Myotrophin | C | protein | 123 | Homo sapiens | P58546 (AlphaFold model) |
>7DSA_1 F-actin-capping protein subunit alpha-1 (chains A) MADFEDRVSDEEKVRIAAKFITHAPPGEFNEVFNDVRLLLNNDNLLREGAAHAFAQYNMD QFTPVKIEGYDDQVLITEHGDLGNGRFLDPRNKISFKFDHLRKEASDPQPEDTESALKQW RDACDSALRAYVKDHYPNGFCTVYGKSIDGQQTIIACIESHQFQPKNFWNGRWRSEWKFT ITPPTAQVAAVLKIQVHYYEDGNVQLVSHKDIQDSVQVSSDVQTAKEFIKIIENAENEYQ TAISENYQTMSDTTFKALRRQLPVTRTKIDWNKILSYKIGKEMQNA
>7DSA_2 F-actin-capping protein subunit beta isoforms 1 (chains B) MSDQQLDCALDLMRRLPPQQIEKNLSDLIDLVPSLCEDLLSSVDQPLKIARDKVVGKDYL LCDYNRDGDSYRSPWSNKYDPPLEDGAMPSARLRKLEVEANNAFDQYRDLYFEGGVSSVY LWDLDHGFAGVILIKKAGDGSKKIKGCWDSIHVVEVQEKSSGRTAHYKLTSTVMLWLQTN KTGSGTMNLGGSLTRQMEKDETVSDSSPHIANIGRLVEDMENKIRSTLNEIYFGKTKDIV NGLR
>7DSA_3 Myotrophin (chains C) GPLGSMCDKEFMWALKNGDLDEVKDYVAKGEDVNRTLEGGRKPLHYAADCGQLEILEFLL LKGADINAPDKHHITPLLSAVYEGHVSCVKLLLSKGADKTVKGPDGLTAFEATDNQAIKA LLQ
| ID | Name | Formula | Copies |
|---|---|---|---|
| MG | Magnesium ion | Mg | 2 |
Structural Insights into the Regulation of Actin Capping Protein by Twinfilin C-terminal Tail. Takeda, S., Koike, R., Fujiwara, I. et al. J Mol Biol (2021) 433:166891-166891. DOI 10.1016/j.jmb.2021.166891 · PubMed
Other PDB entries of the same protein (UniProt P13127 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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