Cryo-EM structure of the undecorated barbed end of filamentous beta/gamma actin. Determined by electron microscopy at 3.59 Å resolution. Released 9 Aug 2023.
Explore 8OI6 in 3D Show helices and sheets RCSB PDB PDBe
8OI6 contains 91 α-helices and 85 β-strands across 6 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 | 8-11 | 4 | 1 |
| β-strand | 16-21 | 6 | 1 |
| β-strand | 29-32 | 4 | 1 |
| β-strand | 35-38 | 4 | 2 |
| β-strand | 53-54 | 2 | 2 |
| α-helix | 56-60 | 5 | |
| β-strand | 65-68 | 4 | 2 |
| β-strand | 71-72 | 2 | 3 |
| β-strand | 75-76 | 2 | 3 |
| α-helix | 79-88 | 10 | |
| α-helix | 89-94 | 6 | |
| β-strand | 103-107 | 5 | 1 |
| α-helix | 113-122 | 10 | |
| α-helix | 123-127 | 5 | |
| β-strand | 131-136 | 6 | 1 |
| α-helix | 137-145 | 9 | |
| β-strand | 149-155 | 7 | 4 |
| β-strand | 160-166 | 7 | 4 |
| β-strand | 169-170 | 2 | 4 |
| β-strand | 176-178 | 3 | 4 |
| α-helix | 182-192 | 11 | |
| α-helix | 193-196 | 4 | |
| α-helix | 203-213 | 11 | |
| α-helix | 223-232 | 10 | |
| β-strand | 238-241 | 4 | 5 |
| β-strand | 247-250 | 4 | 5 |
| α-helix | 252-255 | 4 | |
| α-helix | 258-261 | 4 | |
| α-helix | 264-267 | 4 | |
| α-helix | 272-273 | 2 | |
| α-helix | 274-284 | 11 | |
| α-helix | 290-294 | 5 | |
| β-strand | 297-300 | 4 | 4 |
| α-helix | 302-305 | 4 | |
| α-helix | 309-320 | 12 | |
| β-strand | 329-330 | 2 | 4 |
| α-helix | 335-337 | 3 | |
| α-helix | 338-348 | 11 | |
| α-helix | 351-354 | 4 | |
| β-strand | 357-358 | 2 | 1 |
| α-helix | 359-365 | 7 | |
| α-helix | 367-370 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 8-9 | 2 | 6 |
| β-strand | 10-11 | 2 | 7 |
| β-strand | 16-19 | 4 | 7 |
| β-strand | 29-32 | 4 | 7 |
| β-strand | 35-38 | 4 | 8 |
| α-helix | 41-42 | 2 | |
| β-strand | 53-54 | 2 | 8 |
| α-helix | 56-60 | 5 | |
| β-strand | 65-68 | 4 | 8 |
| β-strand | 71-72 | 2 | 9 |
| β-strand | 75-76 | 2 | 9 |
| α-helix | 79-88 | 10 | |
| α-helix | 89-94 | 6 | |
| β-strand | 103-107 | 5 | 6 |
| α-helix | 113-125 | 13 | |
| β-strand | 131-136 | 6 | 6 |
| α-helix | 137-145 | 9 | |
| β-strand | 149-155 | 7 | 10 |
| β-strand | 160-166 | 7 | 10 |
| β-strand | 169-170 | 2 | 10 |
| α-helix | 172-174 | 3 | |
| β-strand | 176-178 | 3 | 10 |
| α-helix | 182-193 | 12 | |
| α-helix | 203-216 | 14 | |
| α-helix | 223-232 | 10 | |
| β-strand | 238-241 | 4 | 11 |
| β-strand | 247-250 | 4 | 11 |
| α-helix | 253-256 | 4 | |
| α-helix | 258-261 | 4 | |
| α-helix | 264-267 | 4 | |
| α-helix | 272-273 | 2 | |
| α-helix | 274-284 | 11 | |
| α-helix | 287-294 | 8 | |
| β-strand | 297-300 | 4 | 10 |
| α-helix | 302-305 | 4 | |
| α-helix | 309-320 | 12 | |
| β-strand | 329-330 | 2 | 10 |
| α-helix | 335-337 | 3 | |
| α-helix | 338-348 | 11 | |
| α-helix | 350-355 | 6 | |
| β-strand | 357-358 | 2 | 6 |
| α-helix | 359-365 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 8-9 | 2 | 12 |
| β-strand | 10-11 | 2 | 13 |
| β-strand | 16-19 | 4 | 13 |
| β-strand | 29-32 | 4 | 13 |
| β-strand | 35-38 | 4 | 14 |
| β-strand | 42 | 1 | 4 |
| 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 | |
| β-strand | 103-107 | 5 | 12 |
| α-helix | 113-122 | 10 | |
| α-helix | 123-127 | 5 | |
| β-strand | 131-136 | 6 | 12 |
| α-helix | 137-144 | 8 | |
| β-strand | 150-155 | 6 | 16 |
| β-strand | 160-165 | 6 | 16 |
| α-helix | 172-174 | 3 | |
| β-strand | 176-178 | 3 | 16 |
| α-helix | 182-193 | 12 | |
| β-strand | 198 | 1 | 17 |
| α-helix | 203-216 | 14 | |
| α-helix | 223-232 | 10 | |
| β-strand | 238-241 | 4 | 18 |
| β-strand | 247-250 | 4 | 18 |
| α-helix | 253-256 | 4 | |
| α-helix | 258-261 | 4 | |
| α-helix | 264-267 | 4 | |
| α-helix | 272-273 | 2 | |
| α-helix | 274-283 | 10 | |
| α-helix | 289-295 | 7 | |
| β-strand | 297-300 | 4 | 16 |
| α-helix | 302-305 | 4 | |
| α-helix | 309-320 | 12 | |
| β-strand | 329-330 | 2 | 16 |
| α-helix | 335-337 | 3 | |
| α-helix | 338-348 | 11 | |
| α-helix | 352-355 | 4 | |
| β-strand | 357-358 | 2 | 12 |
| α-helix | 359-365 | 7 | |
| α-helix | 367-370 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 8-10 | 3 | 19 |
| β-strand | 11 | 1 | 20 |
| β-strand | 16-19 | 4 | 20 |
| β-strand | 21 | 1 | 19 |
| β-strand | 29-32 | 4 | 20 |
| β-strand | 35-38 | 4 | 21 |
| α-helix | 41-42 | 2 | |
| β-strand | 53-54 | 2 | 21 |
| α-helix | 56-60 | 5 | |
| α-helix | 62-64 | 3 | |
| β-strand | 65-68 | 4 | 21 |
| β-strand | 71 | 1 | 22 |
| β-strand | 76 | 1 | 22 |
| α-helix | 79-87 | 9 | |
| α-helix | 88-94 | 7 | |
| β-strand | 103-107 | 5 | 19 |
| α-helix | 113-121 | 9 | |
| α-helix | 122-126 | 5 | |
| β-strand | 131-136 | 6 | 19 |
| α-helix | 137-144 | 8 | |
| β-strand | 151-155 | 5 | 23 |
| β-strand | 160-163 | 4 | 23 |
| β-strand | 166 | 1 | 24 |
| β-strand | 169 | 1 | 24 |
| β-strand | 176-178 | 3 | 23 |
| α-helix | 182-193 | 12 | |
| β-strand | 198 | 1 | 25 |
| α-helix | 203-216 | 14 | |
| α-helix | 223-232 | 10 | |
| α-helix | 234-236 | 3 | |
| β-strand | 238-241 | 4 | 26 |
| β-strand | 247-250 | 4 | 26 |
| α-helix | 253-256 | 4 | |
| α-helix | 258-260 | 3 | |
| α-helix | 264-267 | 4 | |
| α-helix | 274-284 | 11 | |
| α-helix | 287-289 | 3 | |
| α-helix | 290-295 | 6 | |
| β-strand | 297-300 | 4 | 23 |
| α-helix | 302-305 | 4 | |
| α-helix | 309-320 | 12 | |
| β-strand | 329-330 | 2 | 23 |
| α-helix | 338-348 | 11 | |
| α-helix | 350-353 | 4 | |
| β-strand | 357-358 | 2 | 19 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3 | 1 | 17 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Actin, cytoplasmic 1 | A, B, C, D | protein | 375 | Bos taurus | P60712 (AlphaFold model) |
| Phalloidin | H, I, J | protein | 7 | Amanita phalloides |
>8OI6_1 Actin, cytoplasmic 1 (chains A, B, C, D) MDDDIAALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQS KRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMT QIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVTHTVPIYEGYALPHAILRLDL AGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSY ELPDGQVITIGNERFRCPEALFQPSFLGMESCGIHETTFNSIMKCDVDIRKDLYANTVLS GGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQ EYDESGPSIVHRKCF
>8OI6_2 PHALLOIDIN (chains H, I, J) WXATCPA
Molecular mechanisms of inorganic-phosphate release from the core and barbed end of actin filaments. Oosterheert, W., Blanc, F.E.C., Roy, A. et al. Nat Struct Mol Biol (2023) 30:1774-1785. DOI 10.1038/s41594-023-01101-9 · PubMed
Other PDB entries of the same protein (UniProt P60712 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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