yeast betaprime COP 1-304H6. Determined by X-ray diffraction at 1.8 Å resolution. Released 12 Dec 2012.
Explore 2YNO in 3D Show helices and sheets RCSB PDB PDBe
2YNO contains 7 α-helices and 56 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 | 6-12 | 7 | 1 |
| α-helix | 15 | 1 | |
| β-strand | 16-21 | 6 | 2 |
| β-strand | 27-32 | 6 | 2 |
| β-strand | 36-41 | 6 | 2 |
| β-strand | 46-52 | 7 | 2 |
| β-strand | 58-64 | 7 | 3 |
| α-helix | 65-67 | 3 | |
| β-strand | 69-74 | 6 | 3 |
| β-strand | 78-83 | 6 | 3 |
| β-strand | 89-94 | 6 | 3 |
| β-strand | 100-105 | 6 | 4 |
| β-strand | 111-116 | 6 | 4 |
| β-strand | 121-125 | 5 | 4 |
| α-helix | 126-128 | 3 | |
| β-strand | 131-136 | 6 | 4 |
| β-strand | 143-148 | 6 | 5 |
| β-strand | 155-160 | 6 | 5 |
| β-strand | 164-169 | 6 | 5 |
| β-strand | 177-180 | 4 | 5 |
| β-strand | 189-192 | 4 | 6 |
| β-strand | 200-204 | 5 | 6 |
| β-strand | 209-214 | 6 | 6 |
| β-strand | 220-225 | 6 | 6 |
| β-strand | 231-236 | 6 | 7 |
| β-strand | 242-247 | 6 | 7 |
| β-strand | 251-256 | 6 | 7 |
| β-strand | 262-267 | 6 | 7 |
| β-strand | 273-278 | 6 | 1 |
| α-helix | 283-285 | 3 | |
| β-strand | 286-291 | 6 | 1 |
| β-strand | 294-299 | 6 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 6-12 | 7 | 8 |
| α-helix | 15 | 1 | |
| β-strand | 16-21 | 6 | 9 |
| β-strand | 27-32 | 6 | 9 |
| β-strand | 36-41 | 6 | 9 |
| β-strand | 46-52 | 7 | 9 |
| β-strand | 58-64 | 7 | 10 |
| α-helix | 65-67 | 3 | |
| β-strand | 69-74 | 6 | 10 |
| β-strand | 78-83 | 6 | 10 |
| β-strand | 89-94 | 6 | 10 |
| β-strand | 100-105 | 6 | 11 |
| β-strand | 111-116 | 6 | 11 |
| β-strand | 121-125 | 5 | 11 |
| β-strand | 131-136 | 6 | 11 |
| β-strand | 143-148 | 6 | 12 |
| β-strand | 155-160 | 6 | 12 |
| β-strand | 164-169 | 6 | 12 |
| β-strand | 177-180 | 4 | 12 |
| β-strand | 189-192 | 4 | 13 |
| β-strand | 200-204 | 5 | 13 |
| β-strand | 209-214 | 6 | 13 |
| β-strand | 220-225 | 6 | 13 |
| β-strand | 231-236 | 6 | 14 |
| β-strand | 242-247 | 6 | 14 |
| β-strand | 252-256 | 5 | 14 |
| β-strand | 262-266 | 5 | 14 |
| β-strand | 273-278 | 6 | 8 |
| α-helix | 283-285 | 3 | |
| β-strand | 286-291 | 6 | 8 |
| β-strand | 294-299 | 6 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Coatomer subunit beta' | A, B | protein | 310 | Saccharomyces cerevisiae | P41811 (AlphaFold model) |
| Poly ala | P | protein | 5 | UNIDENTIFIED |
>2YNO_1 Coatomer subunit beta' (chains A, B) MKLDIKKTFSNRSDRVKGIDFHPTEPWVLTTLYSGRVELWNYETQVEVRSIQVTETPVRA GKFIARKNWIIVGSDDFRIRVFNYNTGEKVVDFEAHPDYIRSIAVHPTKPYVLSGSDDLT VKLWNWENNWALEQTFEGHEHFVMCVAFNPKDPSTFASGCLDRTVKVWSLGQSTPNFTLT TGQERGVNYVDYYPLPDKPYMITASDDLTIKIWDYQTKSCVATLEGHMSNVSFAVFHPTL PIIISGSEDGTLKIWNSSTYKVEKTLNVGLERSWCIATHPTGRKNYIASGFDNGFTVLSL GNDEHHHHHH
>2YNO_2 POLY ALA (chains P) XXXXX
Molecular Basis for Recognition of Dilysine Trafficking Motifs by Copi. Jackson, L.P., Lewis, M., Kent, H.M. et al. Dev Cell (2012) 23:1255. DOI 10.1016/J.DEVCEL.2012.10.017 · PubMed
Other PDB entries of the same protein (UniProt P41811 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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