Crystal structure of dictyostelium caatp-actin in complex with gelsolin segment 1. Determined by X-ray diffraction at 2.4 Å resolution. Released 1 Mar 2000.
Explore 1C0F in 3D Show helices and sheets RCSB PDB PDBe
1C0F contains 33 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 |
| α-helix | 56-60 | 5 | |
| α-helix | 62-64 | 3 | |
| β-strand | 65-68 | 4 | 5 |
| β-strand | 71-72 | 2 | 6 |
| β-strand | 75-76 | 2 | 6 |
| α-helix | 79-87 | 9 | |
| α-helix | 88-94 | 7 | |
| α-helix | 98-100 | 3 | |
| β-strand | 103-107 | 5 | 3 |
| α-helix | 113-121 | 9 | |
| α-helix | 122-126 | 5 | |
| 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 | 182-196 | 15 | |
| α-helix | 203-216 | 14 | |
| α-helix | 223-232 | 10 | |
| β-strand | 238-241 | 4 | 8 |
| β-strand | 247-250 | 4 | 8 |
| α-helix | 253-262 | 10 | |
| α-helix | 264-267 | 4 | |
| α-helix | 272-273 | 2 | |
| α-helix | 274-283 | 10 | |
| α-helix | 287-294 | 8 | |
| β-strand | 297-300 | 4 | 7 |
| α-helix | 302-304 | 3 | |
| α-helix | 309-320 | 12 | |
| α-helix | 326-327 | 2 | |
| β-strand | 329-330 | 2 | 7 |
| α-helix | 335-337 | 3 | |
| α-helix | 338-348 | 11 | |
| 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 | 8-12 | 5 | |
| β-strand | 18-25 | 8 | 1 |
| β-strand | 28-31 | 4 | 1 |
| α-helix | 32-33 | 2 | |
| α-helix | 34-36 | 3 | |
| β-strand | 39-41 | 3 | 2 |
| β-strand | 45-53 | 9 | 1 |
| α-helix | 58 | 1 | |
| β-strand | 59-67 | 9 | 1 |
| α-helix | 73-89 | 17 | |
| β-strand | 94-100 | 7 | 1 |
| α-helix | 106-109 | 4 | |
| β-strand | 117-119 | 3 | 2 |
| α-helix | 123-125 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Gelsolin segment 1 | S | protein | 127 | Homo sapiens | P06396 (AlphaFold model) |
| Actin | A | protein | 368 | Dictyostelium discoideum | P07830 (AlphaFold model) |
>1C0F_1 GELSOLIN SEGMENT 1 (chains S) MGSVVEHPEFLKAGKEPGLQIWRVEKFDLVPVPTCLYGDFFTGDAYVILKTVQLRNGNLQ YDLHYWLGNECSQDESGAAAIFTVQLDDYLNGRAVQHREVQGFESATFLGYFKSGLKYKK GGVASGF
>1C0F_2 ACTIN (chains A) DGEDVQALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHTGKDSYVGDEAQSKRGILTL KYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETF NTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVSHTVPIYEGYALPHAILRLDLAGRDLTD YMMKILTERGYSFTTTAEREIVRDIKEKLAYVALDFEAEMQTAASSSALEKSYELPDGQV ITIGNERFRCPEALFQPSFLGMESAGIHETTYNSIMKCDVDIRKDLYGNVVLSGGTTMFP GIADRMNKELTALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKEEYDESGP SIVHRKCF
Structural basis for the higher Ca(2+)-activation of the regulated actin-activated myosin ATPase observed with Dictyostelium/Tetrahymena actin chimeras. Matsuura, Y., Stewart, M., Kawamoto, M. et al. J Mol Biol (2000) 296:579-595. DOI 10.1006/jmbi.1999.3467 · 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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