Structure of the N-terminal 3 domains (V1-V3) villin bound to actin. Determined by X-ray diffraction at 2.69 Å resolution. Released 15 Oct 2025.
Explore 9JW0 in 3D Show helices and sheets RCSB PDB PDBe
9JW0 contains 40 α-helices and 43 β-strands across 2 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 | 15-22 | 8 | 1 |
| β-strand | 25-28 | 4 | 1 |
| α-helix | 29-30 | 2 | |
| α-helix | 31-33 | 3 | |
| β-strand | 36-38 | 3 | 2 |
| β-strand | 42-51 | 10 | 1 |
| β-strand | 54-63 | 10 | 1 |
| α-helix | 69-85 | 17 | |
| β-strand | 91-96 | 6 | 1 |
| α-helix | 102-106 | 5 | |
| β-strand | 114-116 | 3 | 2 |
| α-helix | 120-122 | 3 | |
| β-strand | 125 | 1 | 3 |
| β-strand | 134-139 | 6 | 4 |
| β-strand | 145-148 | 4 | 4 |
| α-helix | 154-156 | 3 | |
| β-strand | 158 | 1 | 5 |
| β-strand | 162-166 | 5 | 4 |
| β-strand | 170-175 | 6 | 4 |
| α-helix | 176 | 1 | |
| α-helix | 181-198 | 18 | |
| β-strand | 202-207 | 6 | 4 |
| α-helix | 218-227 | 10 | |
| α-helix | 233-236 | 4 | |
| β-strand | 238 | 1 | 5 |
| α-helix | 239 | 1 | |
| α-helix | 246-256 | 11 | |
| β-strand | 258-263 | 6 | 6 |
| β-strand | 270-276 | 7 | 6 |
| β-strand | 280 | 1 | 7 |
| α-helix | 281-283 | 3 | |
| β-strand | 289-293 | 5 | 6 |
| α-helix | 295-297 | 3 | |
| β-strand | 299-303 | 5 | 6 |
| α-helix | 309-325 | 17 | |
| β-strand | 334-338 | 5 | 6 |
| α-helix | 344-348 | 5 | |
| β-strand | 352 | 1 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 8-12 | 5 | 8 |
| β-strand | 16-21 | 6 | 8 |
| β-strand | 22 | 1 | 3 |
| β-strand | 24 | 1 | 3 |
| β-strand | 29-32 | 4 | 8 |
| β-strand | 35-38 | 4 | 9 |
| β-strand | 53-54 | 2 | 9 |
| α-helix | 56-60 | 5 | |
| β-strand | 65-68 | 4 | 9 |
| β-strand | 71-72 | 2 | 10 |
| β-strand | 75-76 | 2 | 10 |
| α-helix | 79-87 | 9 | |
| α-helix | 88-94 | 7 | |
| α-helix | 98-100 | 3 | |
| β-strand | 103-107 | 5 | 8 |
| α-helix | 113-125 | 13 | |
| β-strand | 131-136 | 6 | 8 |
| α-helix | 137-144 | 8 | |
| β-strand | 150-155 | 6 | 11 |
| β-strand | 160-166 | 7 | 11 |
| β-strand | 169-170 | 2 | 11 |
| α-helix | 172-174 | 3 | |
| β-strand | 176-178 | 3 | 11 |
| α-helix | 182-196 | 15 | |
| α-helix | 203-216 | 14 | |
| α-helix | 223-232 | 10 | |
| β-strand | 238-241 | 4 | 12 |
| β-strand | 247-250 | 4 | 12 |
| 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 | 287-289 | 3 | |
| α-helix | 290-294 | 5 | |
| β-strand | 297-300 | 4 | 11 |
| α-helix | 302-304 | 3 | |
| α-helix | 309-320 | 12 | |
| α-helix | 326-327 | 2 | |
| β-strand | 329-330 | 2 | 11 |
| α-helix | 335-337 | 3 | |
| α-helix | 338-348 | 11 | |
| α-helix | 352-355 | 4 | |
| β-strand | 357-358 | 2 | 8 |
| α-helix | 359-364 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Villin | A | protein | 400 | Paralvinella sulfincola | |
| Actin, alpha skeletal muscle | B | protein | 377 | Gallus gallus | P68139 (AlphaFold model) |
>9JW0_1 Villin (chains A) TDPAFRSVPKGTPCFLIWRIENFQPVPVPKDQYGNFFEGDAYIILSQKDNKGILEQNLHF WLGKNSSQDEQGTAALKTVELDDYLGGTPVQHRECQNNESKLFLSYFKNKSLKYLQGGVA SGFNHVEHIVRRRLLSVKGKHTPRMEEKPEISWSQMNKGDVFILDLGEIIYVWNGELCSR TERIKAMEIARGMRDDRGTGNIIVVEDGEETPDDMGEEEFEVFNEYLPVADKEASIKSAE EGGADENFEKKKVAQLKLWKVAEEDGNLKITEEATAPLDKKMLDSNDCFIVDNGEDGIWV WTGKKASPKERKESMNNAMAFLKQRNYSSQTRVTKVPEGGESSEFKSLFKTWEKTKLPGS VKPYSVNKIAQTVQTKFDAMTLHNNPEVAKETGMVDDGSG
>9JW0_2 Actin, alpha skeletal muscle (chains B) MCDEDETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEA QSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREK MTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRL DLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEK SYELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNV MSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWIT KQEYDEAGPSIVHRKCF
The structure of an actin nucleus stabilized by villin. Robinson, R.C., Chongrungreang, T., Ponlachantra, K. et al. Sci Adv (2025) 11:eadw6915-eadw6915. DOI 10.1126/sciadv.adw6915 · PubMed
Other PDB entries of the same protein (UniProt P68139 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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