Crystal structure of Actin capping protein. Determined by X-ray diffraction at 1.9 Å resolution. Released 4 Aug 2010.
Explore 3AA7 in 3D Show helices and sheets RCSB PDB PDBe
3AA7 contains 21 α-helices and 21 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 | 10-22 | 13 | |
| α-helix | 24-25 | 2 | |
| α-helix | 29-40 | 12 | |
| α-helix | 43-61 | 19 | |
| β-strand | 64-65 | 2 | 1 |
| β-strand | 74-75 | 2 | 1 |
| α-helix | 78-80 | 3 | |
| β-strand | 81-83 | 3 | 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 | 140-148 | 9 | 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 | 204-217 | 14 | 3 |
| α-helix | 221-249 | 29 | |
| α-helix | 250-254 | 5 | |
| α-helix | 255-258 | 4 | |
| α-helix | 271-274 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 3-13 | 11 | |
| α-helix | 18-20 | 3 | |
| α-helix | 21-31 | 11 | |
| α-helix | 33-35 | 3 | |
| α-helix | 36-42 | 7 | |
| β-strand | 48-52 | 5 | 4 |
| β-strand | 57-61 | 5 | 4 |
| α-helix | 63-65 | 3 | |
| β-strand | 66-67 | 2 | 5 |
| β-strand | 70-72 | 3 | 5 |
| β-strand | 79-80 | 2 | 5 |
| α-helix | 91-112 | 22 | |
| β-strand | 116-124 | 9 | 3 |
| β-strand | 127-137 | 11 | 3 |
| β-strand | 144-158 | 15 | 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 |
| 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 and 2 | B | protein | 244 | Gallus gallus | P14315 (AlphaFold model) |
>3AA7_1 F-actin-capping protein subunit alpha-1 (chains A) MADFEDRVSDEEKVRIAAKFITHAPPGEFNEVFNDVRLLLNNDNLLREGAAHAFAQYNMD QFTPVKIEGYDDQVLITEHGDLGNGRFLDPRNKISFKFDHLRKEASDPQPEDTESALKQW RDACDSALRAYVKDHYPNGFCTVYGKSIDGQQTIIACIESHQFQPKNFWNGRWRSEWKFT ITPPTAQVAAVLKIQVHYYEDGNVQLVSHKDIQDSVQVSSDVQTAKEFIKIIENAENEYQ TAISENYQTMSDTTFKALRRQLPVTRTKIDWNKILSYKIGKEMQNA
>3AA7_2 F-actin-capping protein subunit beta isoforms 1 and 2 (chains B) MSDQQLDCALDLMRRLPPQQIEKNLSDLIDLVPSLCEDLLSSVDQPLKIARDKVVGKDYL LCDYNRDGDSYRSPWSNKYDPPLEDGAMPSARLRKLEVEANNAFDQYRDLYFEGGVSSVY LWDLDHGFAGVILIKKAGDGSKKIKGCWDSIHVVEVQEKSSGRTAHYKLTSTVMLWLQTN KTGSGTMNLGGSLTRQMEKDETVSDSSPHIANIGRLVEDMENKIRSTLNEIYFGKTKDIV NGLR
| ID | Name | Formula | Copies |
|---|---|---|---|
| BA | Barium ion | Ba | 1 |
Water and common crystallization additives (MES) are not listed.
Two distinct mechanisms for actin capping protein regulation--steric and allosteric inhibition. Takeda, S., Minakata, S., Koike, R. et al. PLoS Biol (2010) 8:e1000416-e1000416. DOI 10.1371/journal.pbio.1000416 · 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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