Complex of Dictyostelium discoideum Actin with Profilin and the Last Poly-Pro of Human VASP. Determined by X-ray diffraction at 2.3 Å resolution. Released 19 Aug 2008.
Explore 3CHW in 3D Show helices and sheets RCSB PDB PDBe
3CHW contains 33 α-helices and 26 β-strands across 3 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 | 29-32 | 4 | 1 |
| β-strand | 35-38 | 4 | 2 |
| β-strand | 53-54 | 2 | 2 |
| α-helix | 56-60 | 5 | |
| 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 | 89-93 | 5 | |
| α-helix | 98-100 | 3 | |
| β-strand | 103-107 | 5 | 1 |
| α-helix | 113-121 | 9 | |
| α-helix | 122-126 | 5 | |
| β-strand | 131-136 | 6 | 1 |
| α-helix | 137-144 | 8 | |
| β-strand | 150-155 | 6 | 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 | 182-194 | 13 | |
| α-helix | 203-216 | 14 | |
| α-helix | 223-232 | 10 | |
| β-strand | 238-241 | 4 | 5 |
| β-strand | 247-250 | 4 | 5 |
| α-helix | 253-259 | 7 | |
| α-helix | 264-267 | 4 | |
| α-helix | 271-273 | 3 | |
| α-helix | 274-283 | 10 | |
| α-helix | 290-294 | 5 | |
| β-strand | 297-300 | 4 | 4 |
| α-helix | 302-304 | 3 | |
| α-helix | 309-318 | 10 | |
| β-strand | 329-330 | 2 | 4 |
| α-helix | 335-337 | 3 | |
| α-helix | 338-347 | 10 | |
| α-helix | 350-353 | 4 | |
| α-helix | 356 | 1 | |
| β-strand | 357-358 | 2 | 1 |
| α-helix | 359-365 | 7 | |
| α-helix | 369-373 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 4-11 | 8 | |
| β-strand | 16-23 | 8 | 6 |
| β-strand | 29-33 | 5 | 6 |
| α-helix | 39-41 | 3 | |
| α-helix | 44-51 | 8 | |
| α-helix | 57-61 | 5 | |
| β-strand | 63-65 | 3 | 6 |
| β-strand | 68-76 | 9 | 6 |
| β-strand | 84-89 | 6 | 6 |
| α-helix | 95-97 | 3 | |
| β-strand | 99-104 | 6 | 6 |
| β-strand | 108-114 | 7 | 6 |
| α-helix | 115 | 1 | |
| α-helix | 120-135 | 16 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 203-211 | 9 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Major actin | A | protein | 375 | Dictyostelium discoideum | P07830 (AlphaFold model) |
| Profilin-1 | P | protein | 139 | Homo sapiens | P07737 (AlphaFold model) |
| Vasodilator-stimulated phosphoprotein 16-residue peptide | V | protein | 16 | P50552 (AlphaFold model) |
>3CHW_1 Major actin (chains A) DGEDVQALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHTGVMVGMGQKDSYVGDEAQS KRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMT QIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVSHTVPIYEGYALPHAILRLDL AGRDLTDYMMKILTERGYSFTTTAEREIVRDIKEKLAYVALDFEAEMQTAASSSALEKSY ELPDGQVITIGNERFRCPEALFQPSFLGMESAGIHETTYNSIMKCDVDIRKDLYGNVVLS GGTTMFPGIADRMNKELTALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKE EYDESGPSIVHRKCF
>3CHW_2 Profilin-1 (chains P) AGWNAYIDNLMADGTCQDAAIVGYKDSPSVWAAVPGKTFVNITPAEVGVLVGKDRSSFYV NGLTLGGQKCSVIRDSLLQDGEFSMDLRTKSTGGAPTFNVTVTKTDKTLVLLMGKEGVHG GLINKKCYEMASHLRRSQY
>3CHW_3 Vasodilator-stimulated phosphoprotein 16-residue peptide (chains V) GAGGGPPPAPPLPAAQ
Modulation of actin structure and function by phosphorylation of Tyr-53 and profilin binding. Baek, K., Liu, X., Ferron, F. et al. Proc Natl Acad Sci U S A (2008) 105:11748-11753. DOI 10.1073/pnas.0805852105 · PubMed
Other PDB entries of the same protein (UniProt P07830 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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