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.
Explore 9GO5 in 3D Show helices and sheets RCSB PDB PDBe
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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 8-12 | 5 | 1 |
| β-strand | 16-21 | 6 | 1 |
| β-strand | 29-32 | 4 | 1 |
| β-strand | 35-38 | 4 | 2 |
| β-strand | 42 | 1 | 3 |
| β-strand | 53-54 | 2 | 2 |
| α-helix | 56-60 | 5 | |
| α-helix | 62-64 | 3 | |
| β-strand | 65-68 | 4 | 2 |
| β-strand | 71-72 | 2 | 4 |
| β-strand | 75-76 | 2 | 4 |
| α-helix | 79-88 | 10 | |
| α-helix | 89-93 | 5 | |
| α-helix | 98-100 | 3 | |
| β-strand | 103-107 | 5 | 1 |
| α-helix | 113-121 | 9 | |
| α-helix | 122-126 | 5 | |
| β-strand | 131-136 | 6 | 1 |
| α-helix | 137-144 | 8 | |
| β-strand | 150-155 | 6 | 5 |
| β-strand | 160-166 | 7 | 5 |
| β-strand | 169-170 | 2 | 5 |
| α-helix | 172-174 | 3 | |
| β-strand | 176-178 | 3 | 5 |
| 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 | 6 |
| β-strand | 247-250 | 4 | 6 |
| α-helix | 253-256 | 4 | |
| α-helix | 258-261 | 4 | |
| α-helix | 264-267 | 4 | |
| α-helix | 274-283 | 10 | |
| α-helix | 290-294 | 5 | |
| β-strand | 297-300 | 4 | 5 |
| α-helix | 302-305 | 4 | |
| α-helix | 309-320 | 12 | |
| β-strand | 329-330 | 2 | 5 |
| α-helix | 335-337 | 3 | |
| α-helix | 338-346 | 9 | |
| α-helix | 352-354 | 3 | |
| β-strand | 357-358 | 2 | 1 |
| α-helix | 359-365 | 7 | |
| α-helix | 367-369 | 3 | |
| α-helix | 370-373 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 8-12 | 5 | 13 |
| β-strand | 16-21 | 6 | 13 |
| β-strand | 29-32 | 4 | 13 |
| β-strand | 35-38 | 4 | 14 |
| β-strand | 53-54 | 2 | 14 |
| α-helix | 56-60 | 5 | |
| α-helix | 62-64 | 3 | |
| β-strand | 65-68 | 4 | 14 |
| β-strand | 71-72 | 2 | 15 |
| β-strand | 75-76 | 2 | 15 |
| α-helix | 79-88 | 10 | |
| α-helix | 89-93 | 5 | |
| α-helix | 98-100 | 3 | |
| β-strand | 103-107 | 5 | 13 |
| α-helix | 113-121 | 9 | |
| α-helix | 122-126 | 5 | |
| β-strand | 131-136 | 6 | 13 |
| α-helix | 137-144 | 8 | |
| β-strand | 150-155 | 6 | 9 |
| β-strand | 160-166 | 7 | 9 |
| β-strand | 169-170 | 2 | 9 |
| α-helix | 172-174 | 3 | |
| β-strand | 176-178 | 3 | 9 |
| 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 | 16 |
| β-strand | 247-250 | 4 | 16 |
| α-helix | 253-256 | 4 | |
| α-helix | 258-261 | 4 | |
| α-helix | 264-267 | 4 | |
| α-helix | 274-283 | 10 | |
| α-helix | 290-294 | 5 | |
| β-strand | 297-300 | 4 | 9 |
| α-helix | 302-305 | 4 | |
| α-helix | 309-320 | 12 | |
| β-strand | 329-330 | 2 | 9 |
| α-helix | 335-337 | 3 | |
| α-helix | 338-346 | 9 | |
| α-helix | 352-354 | 3 | |
| β-strand | 357-358 | 2 | 13 |
| α-helix | 359-365 | 7 | |
| α-helix | 367-369 | 3 | |
| α-helix | 370-373 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Actin | A, B, C, D, E | protein | 375 | Saccharomyces cerevisiae | P60010 (AlphaFold model) |
>9GO5_1 Actin (chains A, B, C, D, E) MDSEVAALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGIMVGMGQKDSYVGDEAQS KRGILTLRYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPMNPKSNREKMT QIMFETFNVPAFYVSIQAVLSLYSSGRTTGIVLDSGDGVTHVVPIYAGFSLPHAILRIDL AGRDLTDYLMKILSERGYSFSTTAEREIVRDIKEKLCYVALDFEQEMQTAAQSSSIEKSY ELPDGQVITIGNERFRAPEALFHPSVLGLESAGIDQTTYNSIMKCDVDVRKELYGNIVMS GGTTMFPGIAERMQKEITALAPSSMKVKIIAPPERKYSVWIGGSILASLTTFQQMWISKQ EYDESGPSIVHHKCF
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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