Remodeling of actin filaments by ADF cofilin proteins. Determined by electron microscopy at 9.0 Å resolution. Released 21 Dec 2011.
Explore 3J0S in 3D Show helices and sheets RCSB PDB PDBe
3J0S contains 336 α-helices and 312 β-strands across 24 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 | 17-20 | 4 | 1 |
| β-strand | 29-31 | 3 | 1 |
| β-strand | 35-38 | 4 | 2 |
| α-helix | 40-42 | 3 | |
| β-strand | 53-54 | 2 | 2 |
| α-helix | 57-60 | 4 | |
| 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 | 113-125 | 13 | |
| β-strand | 131-136 | 6 | 1 |
| α-helix | 137-144 | 8 | |
| β-strand | 149-155 | 7 | 4 |
| β-strand | 160-166 | 7 | 4 |
| β-strand | 169-170 | 2 | 4 |
| α-helix | 172-174 | 3 | |
| β-strand | 176-178 | 3 | 4 |
| α-helix | 183-196 | 14 | |
| α-helix | 203-205 | 3 | |
| α-helix | 208-216 | 9 | |
| α-helix | 223-232 | 10 | |
| β-strand | 238 | 1 | 5 |
| β-strand | 250 | 1 | 5 |
| α-helix | 253-262 | 10 | |
| α-helix | 264-266 | 3 | |
| α-helix | 272-273 | 2 | |
| α-helix | 274-284 | 11 | |
| α-helix | 290-295 | 6 | |
| β-strand | 297-300 | 4 | 4 |
| α-helix | 309-320 | 12 | |
| β-strand | 329-330 | 2 | 4 |
| α-helix | 338-345 | 8 | |
| β-strand | 357-358 | 2 | 1 |
| α-helix | 359-365 | 7 | |
| α-helix | 369-373 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 10-20 | 11 | |
| α-helix | 26-29 | 4 | |
| β-strand | 33-40 | 8 | 61 |
| β-strand | 47-56 | 10 | 61 |
| α-helix | 58-62 | 5 | |
| α-helix | 67-73 | 7 | |
| β-strand | 82-86 | 5 | 61 |
| β-strand | 90-92 | 3 | 62 |
| β-strand | 94-95 | 2 | 62 |
| β-strand | 99-104 | 6 | 61 |
| α-helix | 111-119 | 9 | |
| α-helix | 121-126 | 6 | |
| β-strand | 133-137 | 5 | 61 |
| α-helix | 140-144 | 5 | |
| α-helix | 146-153 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Actin, cytoplasmic 1 | A, B, C, D, E, F, G, H, I, J, K, L | protein | 374 | Gallus gallus | P60706 (AlphaFold model) |
| Cofilin-2 | M, N, O, P, Q, R, S, T, U, V, W, X | protein | 166 | Homo sapiens | P23528 (AlphaFold model) |
>3J0S_1 Actin, cytoplasmic 1 (chains A, B, C, D, E, F, G, H, I, J, K, L) DDDIAALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSK RGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQ IMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVTHTVPIYEGYALPHAILRLDLA GRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSYE LPDGQVITIGNERFRCPEALFQPSFLGMESCGIHETTFNSIMKCDVDIRKDLYANTVLSG GTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQE YDESGPSIVHRKCF
>3J0S_2 Cofilin-2 (chains M, N, O, P, Q, R, S, T, U, V, W, X) MASGVAVSDGVIKVFNDMKVRKSSTPEEVKKRKKAVLFCLSEDKKNIILEEGKEILVGDV GQTVDDPYATFVKMLPDKDCRYALYDATYETKESKKEDLVFIFWAPESAPLKSKMIYASS KDAIKKKLTGIKHELQANCYEEVKDRCTLAEKLGGSAVISLEGKPL
Remodeling of actin filaments by ADF/cofilin proteins. Galkin, V.E., Orlova, A., Kudryashov, D.S. et al. Proc Natl Acad Sci U S A (2011) 108:20568-20572. DOI 10.1073/pnas.1110109108 · PubMed
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