Crystal structure of an actin monomer in complex with the nucleator Cordon-Bleu MET72NLE WH2-motif peptide. Determined by X-ray diffraction at 2.0 Å resolution. Released 26 Sept 2018.
Explore 5YPU in 3D Show helices and sheets RCSB PDB PDBe
5YPU contains 51 α-helices and 42 β-strands across 4 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 | 1 |
| β-strand | 16-21 | 6 | 1 |
| β-strand | 24 | 1 | 2 |
| β-strand | 29-32 | 4 | 1 |
| β-strand | 35 | 1 | 3 |
| β-strand | 54 | 1 | 3 |
| α-helix | 56-60 | 5 | |
| β-strand | 68 | 1 | 3 |
| β-strand | 71-72 | 2 | 4 |
| β-strand | 75-76 | 2 | 4 |
| α-helix | 79-88 | 10 | |
| α-helix | 89-93 | 5 | |
| 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 | 182-192 | 11 | |
| α-helix | 193-196 | 4 | |
| α-helix | 203-216 | 14 | |
| α-helix | 223-232 | 10 | |
| β-strand | 238-241 | 4 | 6 |
| α-helix | 246 | 1 | |
| β-strand | 247-250 | 4 | 6 |
| α-helix | 253-259 | 7 | |
| α-helix | 264-267 | 4 | |
| α-helix | 274-283 | 10 | |
| α-helix | 287-294 | 8 | |
| β-strand | 297-300 | 4 | 5 |
| α-helix | 302-304 | 3 | |
| α-helix | 309-320 | 12 | |
| β-strand | 329-330 | 2 | 5 |
| α-helix | 335-337 | 3 | |
| α-helix | 338-348 | 11 | |
| α-helix | 350-355 | 6 | |
| β-strand | 357-358 | 2 | 1 |
| α-helix | 359-365 | 7 | |
| α-helix | 367-371 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 67-76 | 10 | |
| α-helix | 80-83 | 4 | |
| β-strand | 85 | 1 | 2 |
| α-helix | 86 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 8-12 | 5 | 7 |
| β-strand | 16-21 | 6 | 7 |
| β-strand | 24 | 1 | 8 |
| β-strand | 29-32 | 4 | 7 |
| β-strand | 35 | 1 | 9 |
| β-strand | 54 | 1 | 9 |
| α-helix | 56-60 | 5 | |
| α-helix | 66-67 | 2 | |
| β-strand | 68 | 1 | 9 |
| β-strand | 71-72 | 2 | 10 |
| β-strand | 75-76 | 2 | 10 |
| α-helix | 79-87 | 9 | |
| α-helix | 88-93 | 6 | |
| α-helix | 98-100 | 3 | |
| β-strand | 103-107 | 5 | 7 |
| α-helix | 113-125 | 13 | |
| β-strand | 131-136 | 6 | 7 |
| 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 | 182-192 | 11 | |
| α-helix | 193-196 | 4 | |
| α-helix | 203-216 | 14 | |
| α-helix | 223-232 | 10 | |
| β-strand | 238-241 | 4 | 12 |
| β-strand | 247-250 | 4 | 12 |
| α-helix | 253-259 | 7 | |
| α-helix | 264-267 | 4 | |
| α-helix | 274-283 | 10 | |
| α-helix | 287-294 | 8 | |
| β-strand | 297-300 | 4 | 11 |
| α-helix | 302-304 | 3 | |
| α-helix | 309-320 | 12 | |
| β-strand | 329-330 | 2 | 11 |
| α-helix | 338-348 | 11 | |
| α-helix | 350-355 | 6 | |
| β-strand | 357-358 | 2 | 7 |
| α-helix | 359-365 | 7 | |
| α-helix | 367-371 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Actin, alpha skeletal muscle | A, C | protein | 368 | Oryctolagus cuniculus | P68135 (AlphaFold model) |
| Cordon-Bleu WH2 motif | B, D | protein | 22 | Mus musculus | Q5NBX1 (AlphaFold model) |
>5YPU_1 Actin, alpha skeletal muscle (chains A, C) TTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGI LTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREKMTQIMF ETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRLDLAGRD LTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEKSYELPD GQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVMSGGTT MYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWITKQEYDE AGPSIVHR
>5YPU_2 Cordon-Bleu WH2 motif (chains B, D) SLHSALLEAIHSSGGREKLRKV
Structural evidence for the roles of divalent cations in actin polymerization and activation of ATP hydrolysis. Scipion, C.P.M., Ghoshdastider, U., Ferrer, F.J. et al. Proc Natl Acad Sci U S A (2018) 115:10345-10350. DOI 10.1073/pnas.1806394115 · 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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