Structure of S. cerevesiae mApe1 dodecamer. Determined by electron microscopy at 24.0 Å resolution. Released 15 Jun 2016.
Explore 5JM9 in 3D Show helices and sheets RCSB PDB PDBe
5JM9 contains 21 α-helices and 24 β-strands across 1 chain. 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 | 9-18 | 10 | |
| α-helix | 22-34 | 13 | |
| α-helix | 38 | 1 | |
| β-strand | 39-40 | 2 | 1 |
| β-strand | 56-62 | 7 | 1 |
| β-strand | 66-72 | 7 | 1 |
| α-helix | 78-80 | 3 | |
| β-strand | 83-88 | 6 | 1 |
| β-strand | 93-105 | 13 | 2 |
| β-strand | 108-116 | 9 | 2 |
| α-helix | 122-124 | 3 | |
| β-strand | 125 | 1 | 3 |
| β-strand | 129-137 | 9 | 2 |
| β-strand | 146-151 | 6 | 2 |
| β-strand | 158 | 1 | 2 |
| β-strand | 160 | 1 | 3 |
| α-helix | 161-163 | 3 | |
| β-strand | 182-183 | 2 | 2 |
| α-helix | 197-199 | 3 | |
| α-helix | 200-203 | 4 | |
| α-helix | 213-223 | 11 | |
| α-helix | 227-229 | 3 | |
| β-strand | 230-239 | 10 | 2 |
| β-strand | 244-246 | 3 | 4 |
| β-strand | 252-255 | 4 | 4 |
| α-helix | 258-276 | 19 | |
| α-helix | 280-282 | 3 | |
| β-strand | 286-292 | 7 | 1 |
| α-helix | 305-307 | 3 | |
| α-helix | 309-321 | 13 | |
| α-helix | 328-333 | 6 | |
| β-strand | 336-340 | 5 | 1 |
| β-strand | 344 | 1 | 5 |
| α-helix | 345-346 | 2 | |
| α-helix | 351-353 | 3 | |
| α-helix | 355 | 1 | |
| β-strand | 366-370 | 5 | 1 |
| α-helix | 380-393 | 14 | |
| β-strand | 397-401 | 5 | 1 |
| α-helix | 412-420 | 9 | |
| β-strand | 423-428 | 6 | 1 |
| β-strand | 431 | 1 | 5 |
| β-strand | 432 | 1 | 4 |
| β-strand | 439-442 | 4 | 4 |
| α-helix | 445-465 | 21 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Vacuolar aminopeptidase 1 | A | protein | 514 | Saccharomyces cerevisiae | P14904 (AlphaFold model) |
>5JM9_1 Vacuolar aminopeptidase 1 (chains A) MEEQREILEQLKKTLQMLTVEPSKNNQIANEEKEKKENENSWCILEHNYEDIAQEFIDFI YKNPTTYHVVSFFAELLDKHNFKYLSEKSNWQDSIGEDGGKFYTIRNGTNLSAFILGKNW RAEKGVGVIGSHVDALTVKLKPVSFKDTAEGYGRIAVAPYGGTLNELWLDRDLGIGGRLL YKKKGTNEIKSALVDSTPLPVCRIPSLAPHFGKPAEGPFDKEDQTIPVIGFPTPDEEGNE PPTDDEKKSPLFGKHCIHLLRYVAKLAGVEVSELIQMDLDLFDVQKGTIGGIGKHFLFAP RLDDRLCSFAAMIALICYAKDVNTEESDLFSTVTLYDNEEIGSLTRQGAKGGLLESVVER SSSAFTKKPVDLHTVWANSIILSADVNHLYNPNFPEVYLKNHFPVPNVGITLSLDPNGHM ATDVVGTALVEELARRNGDKVQYFQIKNNSRSGGTIGPSLASQTGARTIDLGIAQLSMHS IRAATGSKDVGLGVKFFNGFFKHWRSVYDEFGEL
Higher-order assemblies of oligomeric cargo receptor complexes form the membrane scaffold of the Cvt vesicle. Bertipaglia, C., Schneider, S., Jakobi, A.J. et al. EMBO Rep (2016) 17:1044-1060. DOI 10.15252/embr.201541960 · PubMed
Other PDB entries of the same protein (UniProt P14904 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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