Cryo-EM structure of nonmuscle gamma-actin. Determined by electron microscopy at 3.38 Å resolution. Released 12 Apr 2023.
Explore 8DNF in 3D Show helices and sheets RCSB PDB PDBe
8DNF contains 88 α-helices and 76 β-strands across 4 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 | 7-10 | 4 | 1 |
| β-strand | 15-20 | 6 | 1 |
| β-strand | 28-31 | 4 | 1 |
| β-strand | 34-37 | 4 | 2 |
| β-strand | 52-53 | 2 | 2 |
| α-helix | 55-59 | 5 | |
| β-strand | 64-67 | 4 | 2 |
| β-strand | 70-71 | 2 | 3 |
| β-strand | 74-75 | 2 | 3 |
| α-helix | 79-87 | 9 | |
| α-helix | 88-92 | 5 | |
| β-strand | 102-106 | 5 | 1 |
| α-helix | 114-121 | 8 | |
| α-helix | 122-126 | 5 | |
| β-strand | 130-135 | 6 | 1 |
| α-helix | 136-144 | 9 | |
| β-strand | 149-154 | 6 | 4 |
| β-strand | 159-164 | 6 | 4 |
| β-strand | 169 | 1 | 4 |
| α-helix | 171-173 | 3 | |
| β-strand | 175-177 | 3 | 4 |
| α-helix | 181-192 | 12 | |
| α-helix | 193-195 | 3 | |
| α-helix | 202-215 | 14 | |
| α-helix | 222-231 | 10 | |
| β-strand | 237-240 | 4 | 5 |
| β-strand | 246-249 | 4 | 5 |
| α-helix | 252-255 | 4 | |
| α-helix | 257-260 | 4 | |
| α-helix | 263-266 | 4 | |
| α-helix | 273-282 | 10 | |
| α-helix | 289-293 | 5 | |
| β-strand | 296-299 | 4 | 4 |
| α-helix | 301-304 | 4 | |
| α-helix | 308-319 | 12 | |
| β-strand | 328-329 | 2 | 4 |
| α-helix | 334-336 | 3 | |
| α-helix | 337-346 | 10 | |
| α-helix | 349-351 | 3 | |
| β-strand | 356-357 | 2 | 1 |
| α-helix | 358-372 | 15 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 7-9 | 3 | 16 |
| β-strand | 15-20 | 6 | 16 |
| β-strand | 28-31 | 4 | 16 |
| β-strand | 34-37 | 4 | 17 |
| β-strand | 52-53 | 2 | 17 |
| α-helix | 55-59 | 5 | |
| β-strand | 64-67 | 4 | 17 |
| β-strand | 70-71 | 2 | 18 |
| β-strand | 74-75 | 2 | 18 |
| α-helix | 79-87 | 9 | |
| α-helix | 88-92 | 5 | |
| β-strand | 102-106 | 5 | 16 |
| α-helix | 114-121 | 8 | |
| α-helix | 122-126 | 5 | |
| β-strand | 130-135 | 6 | 16 |
| α-helix | 136-144 | 9 | |
| β-strand | 149-154 | 6 | 19 |
| β-strand | 159-164 | 6 | 19 |
| β-strand | 169 | 1 | 19 |
| α-helix | 171-173 | 3 | |
| β-strand | 175-177 | 3 | 19 |
| α-helix | 181-192 | 12 | |
| α-helix | 193-195 | 3 | |
| α-helix | 202-215 | 14 | |
| α-helix | 222-231 | 10 | |
| β-strand | 237-240 | 4 | 20 |
| β-strand | 246-249 | 4 | 20 |
| α-helix | 252-255 | 4 | |
| α-helix | 257-260 | 4 | |
| α-helix | 263-266 | 4 | |
| α-helix | 273-282 | 10 | |
| α-helix | 289-293 | 5 | |
| β-strand | 296-299 | 4 | 19 |
| α-helix | 301-304 | 4 | |
| α-helix | 308-319 | 12 | |
| β-strand | 328-329 | 2 | 19 |
| α-helix | 334-336 | 3 | |
| α-helix | 337-346 | 10 | |
| α-helix | 349-351 | 3 | |
| β-strand | 356-357 | 2 | 16 |
| α-helix | 358-372 | 15 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Actin, cytoplasmic 2, N-terminally processed | A, B, C, D | protein | 375 | Homo sapiens | P63261 (AlphaFold model) |
>8DNF_1 Actin, cytoplasmic 2, N-terminally processed (chains A, B, C, D) XEEEIAALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQS KRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMT QIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVTHTVPIYEGYALPHAILRLDL AGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSY ELPDGQVITIGNERFRCPEALFQPSFLGMESCGIHETTFNSIMKCDVDIRKDLYANTVLS GGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQ EYDESGPSIVHRKCF
Structural insights into actin isoforms. Arora, A.S., Huang, H.L., Singh, R. et al. Elife (2023) 12. DOI 10.7554/eLife.82015 · PubMed
Other PDB entries of the same protein (UniProt P63261 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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