9GO5: Actin

CryoEM Reconstruction of Yeast ADP-Actin Filament at 2.5 A resolution. Determined by electron microscopy at 2.5 Å resolution. Released 22 Jan 2025.

Method
Electron microscopy
Resolution
2.5 Å
Organism
Saccharomyces cerevisiae
Chains
5
Atoms
14,930
Mol. weight
210.94 kDa
Ligands
MG, ADP
Released
22 Jan 2025

Explore 9GO5 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9GO5 contains 130 α-helices and 98 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, B and E: 26 helices, 20 β-strands

ElementResiduesLengthSheet
β-strand8-1251
β-strand16-2161
β-strand29-3241
β-strand35-3842
β-strand4213
β-strand53-5422
α-helix56-605
α-helix62-643
β-strand65-6842
β-strand71-7224
β-strand75-7624
α-helix79-8810
α-helix89-935
α-helix98-1003
β-strand103-10751
α-helix113-1219
α-helix122-1265
β-strand131-13661
α-helix137-1448
β-strand150-15565
β-strand160-16675
β-strand169-17025
α-helix172-1743
β-strand176-17835
α-helix182-19211
α-helix193-1964
α-helix203-21614
α-helix223-23210
β-strand238-24146
β-strand247-25046
α-helix253-2564
α-helix258-2614
α-helix264-2674
α-helix274-28310
α-helix290-2945
β-strand297-30045
α-helix302-3054
α-helix309-32012
β-strand329-33025
α-helix335-3373
α-helix338-3469
α-helix352-3543
β-strand357-35821
α-helix359-3657
α-helix367-3693
α-helix370-3734
Chains C and D: 26 helices, 19 β-strands
ElementResiduesLengthSheet
β-strand8-12513
β-strand16-21613
β-strand29-32413
β-strand35-38414
β-strand53-54214
α-helix56-605
α-helix62-643
β-strand65-68414
β-strand71-72215
β-strand75-76215
α-helix79-8810
α-helix89-935
α-helix98-1003
β-strand103-107513
α-helix113-1219
α-helix122-1265
β-strand131-136613
α-helix137-1448
β-strand150-15569
β-strand160-16679
β-strand169-17029
α-helix172-1743
β-strand176-17839
α-helix182-19211
α-helix193-1964
α-helix203-21614
α-helix223-23210
β-strand238-241416
β-strand247-250416
α-helix253-2564
α-helix258-2614
α-helix264-2674
α-helix274-28310
α-helix290-2945
β-strand297-30049
α-helix302-3054
α-helix309-32012
β-strand329-33029
α-helix335-3373
α-helix338-3469
α-helix352-3543
β-strand357-358213
α-helix359-3657
α-helix367-3693
α-helix370-3734

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
ActinA, B, C, D, Eprotein375Saccharomyces cerevisiaeP60010 (AlphaFold model)
Sequence of entity 1 (A, B, C, D, E), FASTA
>9GO5_1 Actin (chains A, B, C, D, E)
MDSEVAALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGIMVGMGQKDSYVGDEAQS
KRGILTLRYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPMNPKSNREKMT
QIMFETFNVPAFYVSIQAVLSLYSSGRTTGIVLDSGDGVTHVVPIYAGFSLPHAILRIDL
AGRDLTDYLMKILSERGYSFSTTAEREIVRDIKEKLCYVALDFEQEMQTAAQSSSIEKSY
ELPDGQVITIGNERFRAPEALFHPSVLGLESAGIDQTTYNSIMKCDVDVRKELYGNIVMS
GGTTMFPGIAERMQKEITALAPSSMKVKIIAPPERKYSVWIGGSILASLTTFQQMWISKQ
EYDESGPSIVHHKCF

Ligands and cofactors

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

Primary citation

Cryo-EM reconstruction of yeast ADP-actin filament at 2.5 angstrom resolution. A comparison with vertebrate F-actin. Stevenson, S.R., Tzokov, S.B., Lahiri, I. et al. Structure (2025) 33:435-442.e3. DOI 10.1016/j.str.2024.12.008 · PubMed

Other PDB entries of the same protein (UniProt P60010 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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