Complex between latrunculin a:rabbit muscle alpha actin:human gelsolin domain 1. Determined by X-ray diffraction at 2.0 Å resolution. Released 19 Jul 2000.
Explore 1ESV in 3D Show helices and sheets RCSB PDB PDBe
1ESV contains 28 α-helices and 28 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 | 8-12 | 5 | 3 |
| β-strand | 16-21 | 6 | 3 |
| β-strand | 22 | 1 | 4 |
| β-strand | 24 | 1 | 4 |
| β-strand | 29-32 | 4 | 3 |
| β-strand | 35-38 | 4 | 5 |
| β-strand | 53-54 | 2 | 5 |
| β-strand | 65-68 | 4 | 5 |
| β-strand | 71-72 | 2 | 6 |
| β-strand | 75-76 | 2 | 6 |
| α-helix | 79-88 | 10 | |
| α-helix | 89-93 | 5 | |
| α-helix | 98-100 | 3 | |
| β-strand | 103-107 | 5 | 3 |
| α-helix | 113-125 | 13 | |
| β-strand | 131-136 | 6 | 3 |
| α-helix | 137-144 | 8 | |
| β-strand | 150-155 | 6 | 7 |
| β-strand | 160-166 | 7 | 7 |
| β-strand | 169-170 | 2 | 7 |
| α-helix | 172-174 | 3 | |
| β-strand | 176-178 | 3 | 7 |
| α-helix | 182-192 | 11 | |
| α-helix | 194-196 | 3 | |
| α-helix | 206-216 | 11 | |
| α-helix | 223-230 | 8 | |
| β-strand | 238-241 | 4 | 8 |
| β-strand | 247-250 | 4 | 8 |
| α-helix | 259-262 | 4 | |
| α-helix | 264-267 | 4 | |
| α-helix | 271-273 | 3 | |
| α-helix | 274-283 | 10 | |
| α-helix | 287-289 | 3 | |
| α-helix | 290-294 | 5 | |
| β-strand | 297-300 | 4 | 7 |
| α-helix | 302-304 | 3 | |
| α-helix | 309-320 | 12 | |
| β-strand | 329-330 | 2 | 7 |
| α-helix | 338-346 | 9 | |
| α-helix | 350-352 | 3 | |
| β-strand | 357-358 | 2 | 3 |
| α-helix | 359-365 | 7 | |
| α-helix | 366-369 | 4 | |
| α-helix | 370-373 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 6-10 | 5 | |
| β-strand | 16-23 | 8 | 1 |
| β-strand | 26-29 | 4 | 1 |
| α-helix | 30-31 | 2 | |
| α-helix | 32-34 | 3 | |
| β-strand | 37-39 | 3 | 2 |
| β-strand | 43-51 | 9 | 1 |
| β-strand | 57-65 | 9 | 1 |
| α-helix | 71-87 | 17 | |
| β-strand | 92-98 | 7 | 1 |
| α-helix | 104-107 | 4 | |
| β-strand | 115-117 | 3 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Gelsolin | S | protein | 125 | Homo sapiens | P06396 (AlphaFold model) |
| Alpha actin | A | protein | 377 | Oryctolagus cuniculus | P68135 (AlphaFold model) |
>1ESV_1 GELSOLIN (chains S) MVVEHPEFLKAGKEPGLQIWRVEKFDLVPVPTCLYGDFFTGDAYVILKTVQLRNGNLQYD LHYWLGNECSQDESGAAAIFTVQLDDYLNGRAVQHREVQGFESATFLGYFKSGLKYKKGG VASGF
>1ESV_2 ALPHA ACTIN (chains A) MCDEDETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEA QSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREK MTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRL DLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEK SYELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNV MSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWIT KQEYDEAGPSIVHRKCF
| ID | Name | Formula | Copies |
|---|---|---|---|
| CA | Calcium ion | Ca | 3 |
| ATP | Adenosine-5'-triphosphate | C10 H16 N5 O13 P3 | 1 |
| LAR | Latrunculin a | C22 H31 N O5 S | 1 |
Latrunculin alters the actin-monomer subunit interface to prevent polymerization. Morton, W.M., Ayscough, K.R., McLaughlin, P.J. Nat Cell Biol (2000) 2:376-378. DOI 10.1038/35014075 · PubMed
Other PDB entries of the same protein (UniProt P06396 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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