Crystal structure of yeast Sec13/31 vertex element of the COPII vesicular coat. Determined by X-ray diffraction at 3.3 Å resolution. Released 3 Jul 2007.
Explore 2PM9 in 3D Show helices and sheets RCSB PDB PDBe
2PM9 contains 7 α-helices and 68 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 | 6-9 | 4 | 1 |
| β-strand | 12 | 1 | 2 |
| β-strand | 15 | 1 | 3 |
| β-strand | 22-25 | 4 | 3 |
| β-strand | 26 | 1 | 2 |
| β-strand | 28 | 1 | 4 |
| β-strand | 43-46 | 4 | 3 |
| α-helix | 50-52 | 3 | |
| β-strand | 65-70 | 6 | 4 |
| β-strand | 77-81 | 5 | 4 |
| β-strand | 86-89 | 4 | 4 |
| β-strand | 100-103 | 4 | 4 |
| β-strand | 113-116 | 4 | 5 |
| β-strand | 123 | 1 | 6 |
| β-strand | 124-127 | 4 | 5 |
| β-strand | 133-134 | 2 | 5 |
| β-strand | 135 | 1 | 7 |
| β-strand | 137 | 1 | 6 |
| β-strand | 151 | 1 | 7 |
| β-strand | 165-168 | 4 | 8 |
| β-strand | 175-179 | 5 | 8 |
| β-strand | 185-189 | 5 | 8 |
| β-strand | 194-199 | 6 | 8 |
| α-helix | 209-211 | 3 | |
| β-strand | 212-217 | 6 | 9 |
| β-strand | 224-229 | 6 | 9 |
| β-strand | 239-241 | 3 | 9 |
| β-strand | 250 | 1 | 9 |
| β-strand | 260-265 | 6 | 10 |
| β-strand | 273-277 | 5 | 10 |
| β-strand | 281-285 | 5 | 10 |
| β-strand | 292-297 | 6 | 10 |
| β-strand | 306-308 | 3 | 1 |
| β-strand | 315-318 | 4 | 1 |
| β-strand | 324-329 | 6 | 1 |
| β-strand | 385-387 | 3 | 11 |
| β-strand | 391-393 | 3 | 11 |
| β-strand | 395 | 1 | 12 |
| β-strand | 402 | 1 | 12 |
| β-strand | 405 | 1 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4 | 1 | 12 |
| α-helix | 11 | 1 | |
| β-strand | 12-15 | 4 | 13 |
| β-strand | 25-28 | 4 | 13 |
| β-strand | 32-39 | 8 | 13 |
| β-strand | 42-50 | 9 | 13 |
| β-strand | 56-61 | 6 | 14 |
| α-helix | 62-63 | 2 | |
| α-helix | 64-66 | 3 | |
| β-strand | 69-74 | 6 | 14 |
| β-strand | 79-83 | 5 | 14 |
| α-helix | 85-87 | 3 | |
| β-strand | 90-95 | 6 | 14 |
| β-strand | 102-107 | 6 | 15 |
| α-helix | 108-109 | 2 | |
| β-strand | 115-120 | 6 | 15 |
| β-strand | 124-129 | 6 | 15 |
| β-strand | 139-142 | 4 | 15 |
| β-strand | 148-150 | 3 | 16 |
| β-strand | 153 | 1 | 16 |
| β-strand | 172-177 | 6 | 16 |
| β-strand | 182-186 | 5 | 16 |
| β-strand | 195-196 | 2 | 16 |
| β-strand | 209-212 | 4 | 17 |
| β-strand | 220-226 | 7 | 17 |
| β-strand | 230-231 | 2 | 17 |
| β-strand | 232 | 1 | 18 |
| β-strand | 234-236 | 3 | 17 |
| β-strand | 244 | 1 | 17 |
| β-strand | 247 | 1 | 18 |
| β-strand | 259-262 | 4 | 19 |
| β-strand | 269-272 | 4 | 19 |
| β-strand | 278-281 | 4 | 19 |
| β-strand | 282 | 1 | 20 |
| β-strand | 290 | 1 | 20 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protein transport protein SEC31 | A | protein | 416 | Saccharomyces cerevisiae | P38968 (AlphaFold model) |
| Protein transport protein SEC13 | B | protein | 297 | Saccharomyces cerevisiae | Q04491 (AlphaFold model) |
>2PM9_1 Protein transport protein SEC31 (chains A) GAMGSMVKLAEFSRTATFAWSHDKIPLLVSGTVSGTVDANFSTDSSLELWSLLAADSEKP IASLQVDSKFNDLDWSHNNKIIAGALDNGSLELYSTNEANNAINSMARFSNHSSSVKTVK FNAKQDNVLASGGNNGEIFIWDMNKCTESPSNYTPLTPGQSMSSVDEVISLAWNQSLAHV FASAGSSNFASIWDLKAKKEVIHLSYTSPNSGIKQQLSVVEWHPKNSTRVATATGSDNDP SILIWDLRNANTPLQTLNQGHQKGILSLDWCHQDEHLLLSSGRDNTVLLWNPESAEQLSQ FPARGNWCFKTKFAPEAPDLFACASFDNKIEVQTLQNLTNTLDEQETETKQQESETDFWN NVSREESKEKPSVFHLQAPTWYGEPSPAAHWAFGGKLVQITPDGKGVSITNPKISG
>2PM9_2 Protein transport protein SEC13 (chains B) MVVIANAHNEMIHDAVMDYYGKRMATCSSDKTIKIFEVEGETHKLIDTLTGHEGPVWRVD WAHPKFGTILASCSYDGKVMIWKEENGRWSQIAVHAVHSASVNSVQWAPHEYGPMLLVAS SDGKVSVVEFKENGTTSPIIIDAHAIGVNSASWAPATIEEDGEHNGTKESRKFVTGGADN LVKIWKYNSDAQTYVLESTLEGHSDWVRDVAWSPTVLLRSYMASVSQDRTCIIWTQDNEQ GPWKKTLLKEEKFPDVLWRASWSLSGNVLALSGGDNKVTLWKENLEGKWEPAGEVHQ
Structure and Organization of Coat Proteins in the COPII Cage. Fath, S., Mancias, J.D., Bi, X. et al. Cell (2007) 129:1325-1336. DOI 10.1016/j.cell.2007.05.036 · PubMed
Other PDB entries of the same protein (UniProt P38968 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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