9QEW: Undecorated actin filament in the ADP-Pi state

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.

Method
Electron microscopy
Resolution
2.18 Å
Organism
Homo sapiens
Chains
5
Atoms
15,280
Mol. weight
210.89 kDa
Ligands
PO4, MG, ADP
Released
8 Oct 2025

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

Secondary structure: helices and β-sheets

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.

Chains A and B: 26 helices, 21 β-strands

ElementResiduesLengthSheet
β-strand8-1258
β-strand16-2168
β-strand2219
β-strand2419
β-strand29-3248
β-strand35-38410
β-strand53-54210
α-helix56-605
α-helix62-643
β-strand65-68410
β-strand71-72211
β-strand75-76211
α-helix79-879
α-helix88-947
α-helix98-1003
β-strand103-10758
α-helix113-12513
β-strand131-13668
α-helix137-1448
β-strand150-15564
β-strand160-16674
β-strand169-17024
α-helix172-1743
β-strand176-17834
α-helix182-19211
α-helix193-1964
α-helix203-21614
α-helix223-23210
β-strand238-241412
β-strand247-250412
α-helix253-2597
α-helix264-2674
α-helix272-2732
α-helix274-28310
α-helix287-2893
α-helix290-2945
β-strand297-30044
α-helix302-3043
α-helix309-32012
β-strand329-33024
α-helix335-3373
α-helix338-3469
α-helix350-3523
β-strand357-35828
α-helix359-3635
α-helix367-3693
α-helix370-3734
Chains C, D and E: 26 helices, 22 β-strands
ElementResiduesLengthSheet
β-strand8-1251
β-strand16-2161
β-strand2212
β-strand2412
β-strand29-3241
β-strand35-3843
β-strand4214
β-strand53-5423
α-helix56-605
α-helix62-643
β-strand65-6843
β-strand71-7225
β-strand75-7625
α-helix79-879
α-helix88-947
α-helix98-1003
β-strand103-10751
α-helix113-12513
β-strand131-13661
α-helix137-1448
β-strand150-15566
β-strand160-16676
β-strand169-17026
α-helix172-1743
β-strand176-17836
α-helix182-19211
α-helix193-1964
α-helix203-21614
α-helix223-23210
β-strand238-24147
β-strand247-25047
α-helix253-2597
α-helix264-2674
α-helix272-2732
α-helix274-28310
α-helix287-2893
α-helix290-2945
β-strand297-30046
α-helix302-3043
α-helix309-32012
β-strand329-33026
α-helix335-3373
α-helix338-3469
α-helix350-3523
β-strand357-35821
α-helix359-3635
α-helix367-3693
α-helix370-3734

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Actin, cytoplasmic 1, N-terminally processedA, B, C, D, Eprotein374Homo sapiensP60709 (AlphaFold model)
Sequence of entity 1 (A, B, C, D, E), FASTA
>9QEW_1 Actin, cytoplasmic 1, N-terminally processed (chains A, B, C, D, E)
DDDIAALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSK
RGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQ
IMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVTHTVPIYEGYALPHAILRLDLA
GRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSYE
LPDGQVITIGNERFRCPEALFQPSFLGMESAGIHETTFNSIMKCDVDIRKDLYANTVLSG
GTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQE
YDESGPSIVHRKCF

Ligands and cofactors

IDNameFormulaCopies
PO4Phosphate ionO4 P5
MGMagnesium ionMg5
ADPAdenosine-5'-diphosphateC10 H15 N5 O10 P25

Primary citation

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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