Cryo-EM structure of the undecorated actin filament in the ADP-Pi state. Determined by electron microscopy at 2.18 Å resolution. Released 8 Oct 2025.
Explore 9QEW in 3D Show helices and sheets RCSB PDB PDBe
9QEW contains 130 α-helices and 108 β-strands across 5 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 |
|---|---|---|---|
| β-strand | 8-12 | 5 | 8 |
| β-strand | 16-21 | 6 | 8 |
| β-strand | 22 | 1 | 9 |
| β-strand | 24 | 1 | 9 |
| β-strand | 29-32 | 4 | 8 |
| β-strand | 35-38 | 4 | 10 |
| β-strand | 53-54 | 2 | 10 |
| α-helix | 56-60 | 5 | |
| α-helix | 62-64 | 3 | |
| β-strand | 65-68 | 4 | 10 |
| β-strand | 71-72 | 2 | 11 |
| β-strand | 75-76 | 2 | 11 |
| α-helix | 79-87 | 9 | |
| α-helix | 88-94 | 7 | |
| α-helix | 98-100 | 3 | |
| β-strand | 103-107 | 5 | 8 |
| α-helix | 113-125 | 13 | |
| β-strand | 131-136 | 6 | 8 |
| α-helix | 137-144 | 8 | |
| β-strand | 150-155 | 6 | 4 |
| β-strand | 160-166 | 7 | 4 |
| β-strand | 169-170 | 2 | 4 |
| α-helix | 172-174 | 3 | |
| β-strand | 176-178 | 3 | 4 |
| α-helix | 182-192 | 11 | |
| α-helix | 193-196 | 4 | |
| α-helix | 203-216 | 14 | |
| α-helix | 223-232 | 10 | |
| β-strand | 238-241 | 4 | 12 |
| β-strand | 247-250 | 4 | 12 |
| α-helix | 253-259 | 7 | |
| 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 | 4 |
| α-helix | 302-304 | 3 | |
| α-helix | 309-320 | 12 | |
| β-strand | 329-330 | 2 | 4 |
| α-helix | 335-337 | 3 | |
| α-helix | 338-346 | 9 | |
| α-helix | 350-352 | 3 | |
| β-strand | 357-358 | 2 | 8 |
| α-helix | 359-363 | 5 | |
| α-helix | 367-369 | 3 | |
| α-helix | 370-373 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 8-12 | 5 | 1 |
| β-strand | 16-21 | 6 | 1 |
| β-strand | 22 | 1 | 2 |
| β-strand | 24 | 1 | 2 |
| β-strand | 29-32 | 4 | 1 |
| β-strand | 35-38 | 4 | 3 |
| β-strand | 42 | 1 | 4 |
| 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 | 5 |
| β-strand | 75-76 | 2 | 5 |
| 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 | 6 |
| β-strand | 160-166 | 7 | 6 |
| β-strand | 169-170 | 2 | 6 |
| α-helix | 172-174 | 3 | |
| β-strand | 176-178 | 3 | 6 |
| α-helix | 182-192 | 11 | |
| α-helix | 193-196 | 4 | |
| α-helix | 203-216 | 14 | |
| α-helix | 223-232 | 10 | |
| β-strand | 238-241 | 4 | 7 |
| β-strand | 247-250 | 4 | 7 |
| α-helix | 253-259 | 7 | |
| 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 | 6 |
| α-helix | 302-304 | 3 | |
| α-helix | 309-320 | 12 | |
| β-strand | 329-330 | 2 | 6 |
| α-helix | 335-337 | 3 | |
| α-helix | 338-346 | 9 | |
| α-helix | 350-352 | 3 | |
| β-strand | 357-358 | 2 | 1 |
| α-helix | 359-363 | 5 | |
| α-helix | 367-369 | 3 | |
| α-helix | 370-373 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Actin, cytoplasmic 1, N-terminally processed | A, B, C, D, E | protein | 374 | Homo sapiens | P60709 (AlphaFold model) |
>9QEW_1 Actin, cytoplasmic 1, N-terminally processed (chains A, B, C, D, E) DDDIAALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSK RGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQ IMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVTHTVPIYEGYALPHAILRLDLA GRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSYE LPDGQVITIGNERFRCPEALFQPSFLGMESAGIHETTFNSIMKCDVDIRKDLYANTVLSG GTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQE YDESGPSIVHRKCF
| ID | Name | Formula | Copies |
|---|---|---|---|
| PO4 | Phosphate ion | O4 P | 5 |
| MG | Magnesium ion | Mg | 5 |
| ADP | Adenosine-5'-diphosphate | C10 H15 N5 O10 P2 | 5 |
Choreography of rapid actin filament disassembly by coronin, cofilin, and AIP1. Oosterheert, W., Boiero Sanders, M., Hofnagel, O. et al. Cell (2025) 188:6845. DOI 10.1016/j.cell.2025.09.016 · PubMed
Other PDB entries of the same protein (UniProt P60709 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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