Actin Complex With a Chimera of Tropomodulin-1 and Leiomodin-1 Actin-Binding Site 2. Determined by X-ray diffraction at 2.4 Å resolution. Released 21 Oct 2015.
Explore 4Z94 in 3D Show helices and sheets RCSB PDB PDBe
4Z94 contains 36 α-helices and 33 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 |
|---|---|---|---|
| α-helix | 6-7 | 2 | |
| β-strand | 8-12 | 5 | 1 |
| β-strand | 16-21 | 6 | 1 |
| β-strand | 22 | 1 | 2 |
| β-strand | 24 | 1 | 2 |
| β-strand | 29-32 | 4 | 1 |
| β-strand | 35-38 | 4 | 3 |
| α-helix | 39 | 1 | |
| β-strand | 53-54 | 2 | 3 |
| α-helix | 55-60 | 6 | |
| β-strand | 65-68 | 4 | 3 |
| β-strand | 71-72 | 2 | 4 |
| β-strand | 75-76 | 2 | 4 |
| α-helix | 79-87 | 9 | |
| α-helix | 88-93 | 6 | |
| α-helix | 98-100 | 3 | |
| β-strand | 103-107 | 5 | 1 |
| α-helix | 113-125 | 13 | |
| 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 | 182-194 | 13 | |
| 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 | 259-262 | 4 | |
| α-helix | 264-267 | 4 | |
| α-helix | 274-283 | 10 | |
| α-helix | 290-295 | 6 | |
| β-strand | 297-300 | 4 | 5 |
| α-helix | 302-304 | 3 | |
| α-helix | 309-320 | 12 | |
| β-strand | 329-330 | 2 | 5 |
| α-helix | 338-346 | 9 | |
| α-helix | 350-354 | 5 | |
| β-strand | 357-358 | 2 | 1 |
| α-helix | 359-365 | 7 | |
| α-helix | 369-373 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 6-10 | 5 | |
| β-strand | 16-23 | 8 | 7 |
| β-strand | 26-29 | 4 | 7 |
| α-helix | 30-31 | 2 | |
| α-helix | 32-34 | 3 | |
| β-strand | 37-39 | 3 | 8 |
| β-strand | 43-51 | 9 | 7 |
| β-strand | 57-65 | 9 | 7 |
| α-helix | 71-87 | 17 | |
| β-strand | 92-98 | 7 | 7 |
| α-helix | 104-107 | 4 | |
| β-strand | 115-117 | 3 | 8 |
| α-helix | 121-123 | 3 | |
| α-helix | 1183-1191 | 9 | |
| β-strand | 1199-1201 | 3 | 9 |
| α-helix | 1210-1220 | 11 | |
| β-strand | 1228-1365 | 3 | 9 |
| α-helix | 1373-1385 | 13 | |
| β-strand | 1391-1393 | 3 | 9 |
| α-helix | 1401-1410 | 10 | |
| α-helix | 1411-1413 | 3 | |
| β-strand | 1419-1421 | 3 | 9 |
| α-helix | 1431-1440 | 10 | |
| β-strand | 1449-1451 | 3 | 9 |
| α-helix | 1457-1482 | 26 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Actin, alpha skeletal muscle | A | protein | 377 | Oryctolagus cuniculus | P68135 (AlphaFold model) |
| Gelsolin, Tropomodulin-1, Leiomodin-1 chimera | G | protein | 326 | Homo sapiens | P06396 (AlphaFold model), P28289 (AlphaFold model), P29536 (AlphaFold model) |
>4Z94_1 Actin, alpha skeletal muscle (chains A) MCDEDETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEA QSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREK MTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRL DLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEK SYELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNV MSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWIT KQEYDEAGPSIVHRKCF
>4Z94_2 Gelsolin, Tropomodulin-1, Leiomodin-1 chimera (chains G) MVVEHPEFLKAGKEPGLQIWRVEKFDLVPVPTNLYGDFFTGDAYVILKTVQLRNGNLQYD LHYWLGNECSQDESGAAAIFTVQLDDYLNGRAVQHREVQGFESATFLGYFKSGLKYKKGG VASGFGGSGGSGGSGLNSVIKPTQYKPVPDEEPNSTDVEETLERIKNNDPKLEEVNLNNI RNIPIPTLKAYAEALKENSYVKKFALANTRADDHVAFAIAIMLKANKTITSLNLDSNHIT GKGILAIFRALLQNNTLTELRFHNQRHICGGKTEMEIAKLLKENTTLLKLGYHFELAGPR MTVTNLLSRNMDKQRQKRLQEQRQAQ
How Leiomodin and Tropomodulin use a common fold for different actin assembly functions. Boczkowska, M., Rebowski, G., Kremneva, E. et al. Nat Commun (2015) 6:8314-8314. DOI 10.1038/ncomms9314 · PubMed
Other PDB entries of the same protein (UniProt P68135 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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