Structure of retromer VPS26-VPS35 subunits bound to SNX3 and DMT1. Determined by X-ray diffraction at 3.2 Å resolution. Released 7 Dec 2016.
Explore 5F0L in 3D Show helices and sheets RCSB PDB PDBe
5F0L contains 48 α-helices and 32 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 |
|---|---|---|---|
| α-helix | 14-36 | 23 | |
| α-helix | 39-51 | 13 | |
| α-helix | 52-54 | 3 | |
| α-helix | 60-86 | 27 | |
| α-helix | 90-91 | 2 | |
| α-helix | 94-98 | 5 | |
| α-helix | 104-121 | 18 | |
| α-helix | 123-125 | 3 | |
| α-helix | 126-136 | 11 | |
| α-helix | 137-139 | 3 | |
| β-strand | 140 | 1 | 1 |
| α-helix | 143-157 | 15 | |
| α-helix | 176-196 | 21 | |
| α-helix | 206-228 | 23 | |
| α-helix | 235-237 | 3 | |
| α-helix | 238-242 | 5 | |
| α-helix | 243-253 | 11 | |
| α-helix | 256-269 | 14 | |
| α-helix | 272-277 | 6 | |
| α-helix | 279-286 | 8 | |
| α-helix | 295-310 | 16 | |
| α-helix | 324-338 | 15 | |
| α-helix | 344-361 | 18 | |
| α-helix | 366-382 | 17 | |
| α-helix | 393-408 | 16 | |
| α-helix | 413-416 | 4 | |
| α-helix | 423-427 | 5 | |
| α-helix | 430-446 | 17 | |
| α-helix | 448-453 | 6 | |
| α-helix | 454-468 | 15 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 12-18 | 7 | 2 |
| β-strand | 26-30 | 5 | 3 |
| α-helix | 32-34 | 3 | |
| β-strand | 36-42 | 7 | 3 |
| β-strand | 48-56 | 9 | 2 |
| β-strand | 63-65 | 3 | 4 |
| β-strand | 68-78 | 11 | 3 |
| α-helix | 82-84 | 3 | |
| β-strand | 85-96 | 12 | 3 |
| β-strand | 99-101 | 3 | 4 |
| β-strand | 105-111 | 7 | 2 |
| β-strand | 121-122 | 2 | 3 |
| β-strand | 126-136 | 11 | 3 |
| β-strand | 143-151 | 9 | 3 |
| β-strand | 155 | 1 | 5 |
| α-helix | 156-158 | 3 | |
| α-helix | 162-163 | 2 | |
| β-strand | 164-170 | 7 | 6 |
| β-strand | 174-180 | 7 | 6 |
| β-strand | 184-186 | 3 | 7 |
| β-strand | 190-200 | 11 | 6 |
| β-strand | 204-219 | 16 | 1 |
| β-strand | 222-237 | 16 | 1 |
| β-strand | 245-251 | 7 | 6 |
| α-helix | 252-255 | 4 | |
| α-helix | 258-260 | 3 | |
| β-strand | 261-264 | 4 | 1 |
| β-strand | 268-280 | 13 | 1 |
| β-strand | 285-288 | 4 | 1 |
| β-strand | 291-292 | 2 | 1 |
| β-strand | 293-295 | 3 | 7 |
| β-strand | 297 | 1 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 14-17 | 4 | |
| α-helix | 18-22 | 5 | |
| α-helix | 24-25 | 2 | |
| β-strand | 29-39 | 11 | 8 |
| α-helix | 42-44 | 3 | |
| β-strand | 46-55 | 10 | 8 |
| β-strand | 64-70 | 7 | 8 |
| α-helix | 71-80 | 10 | |
| α-helix | 81-85 | 5 | |
| α-helix | 89-92 | 4 | |
| α-helix | 97-100 | 4 | |
| α-helix | 108-110 | 3 | |
| α-helix | 112-131 | 20 | |
| α-helix | 133-137 | 5 | |
| α-helix | 139-146 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 554-556 | 3 | 1 |
| α-helix | 557 | 1 | |
| β-strand | 558-559 | 2 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Vacuolar protein sorting-associated protein 35 | A | protein | 462 | Homo sapiens | Q96QK1 (AlphaFold model) |
| Vacuolar protein sorting-associated protein 26A | B | protein | 317 | Homo sapiens | O75436 (AlphaFold model) |
| Sorting nexin-3 | C | protein | 167 | Homo sapiens | O60493 (AlphaFold model) |
| Natural resistance-associated macrophage protein 2 | D | protein | 24 | Homo sapiens | P49281 (AlphaFold model) |
>5F0L_1 Vacuolar protein sorting-associated protein 35 (chains A) GAMGSKLLDEAIQAVKVQSFQMKRCLDKNKLMDALKHASNMLGELRTSMLSPKSYYELYM AISDELHYLEVYLTDEFAKGRKVADLYELVQYAGNIIPRLYLLITVGVVYVKSFPQSRKD ILKDLVEMCRGVQHPLRGLFLRNYLLQCTRNILPDEGEPTDEETTGDISDSMDFVLLNFA EMNKLWVRMQHQGHSRDREKRERERQELRILVGTNLVRLSQLEGVNVERYKQIVLTGILE QVVNCRDALAQEYLMECIIQVFPDEFHLQTLNPFLRACAELHQNVNVKNIIIALIDRLAL FAHREDGPGIPADIKLFDIFSQQVATVIQSRQDMPSEDVVSLQVSLINLAMKCYPDRVDY VDKVLETTVEIFNKLNLEHIATSSAVSKELTRLLKIPVDTYNNILTVLKLKHFHPLFEYF DYESRKSMSCYVLSNVLDYNTEIVSQDQVDSIMNLVSTLIQD
>5F0L_2 Vacuolar protein sorting-associated protein 26A (chains B) MSFLGGFFGPICEIDIVLNDGETRKMAEMKTEDGKVEKHYLFYDGESVSGKVNLAFKQPG KRLEHQGIRIEFVGQIELFNDKSNTHEFVNLVKELALPGELTQSRSYDFEFMQVEKPYES YIGANVRLRYFLKVTIVRRLTDLVKEYDLIVHQLATYPDVNNSIKMEVGIEDCLHIEFEY NKSKYHLKDVIVGKIYFLLVRIKIQHMELQLIKKEITGIGPSTTTETETIAKYEIMDGAP VKGESIPIRLFLAGYDPTPTMRDVNKKFSVRYFLNLVLVDEEDRRYFKQQEIILWRKAPE KLRKQRTNFHQRFESPE
>5F0L_3 Sorting nexin-3 (chains C) GAMGSMAETVADTRRLITKPQNLNDAYGPPSNFLEIDVSNPQTVGVGRGRFTTYEIRVKT NLPIFKLKESTVRRRYSDFEWLRSELERESKVVVPPLPGKAFLRQLPFRGDDGIFDDNFI EERKQGLEQFINKVAGHPLAQNERCLHMFLQDEIIDKSYTPSKIRHA
>5F0L_4 Natural resistance-associated macrophage protein 2 (chains D) HLGLTAQPELYLLNTMDADSLVSR
Structural Mechanism for Cargo Recognition by the Retromer Complex. Lucas, M., Gershlick, D.C., Vidaurrazaga, A. et al. Cell (2016) 167:1623-1635.e14. DOI 10.1016/j.cell.2016.10.056 · PubMed
Other PDB entries of the same protein (UniProt Q96QK1 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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