Mouse retromer (VPS26/VPS35/VPS29) heterotrimer. Determined by electron microscopy at 5.7 Å resolution. Released 19 Feb 2020.
Explore 6VAC in 3D Show helices and sheets RCSB PDB PDBe
6VAC contains 47 α-helices and 46 β-strands across 3 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 | 17-35 | 19 | |
| α-helix | 39-50 | 12 | |
| α-helix | 51-54 | 4 | |
| α-helix | 60-86 | 27 | |
| α-helix | 94-97 | 4 | |
| α-helix | 104-120 | 17 | |
| α-helix | 123-125 | 3 | |
| α-helix | 126-136 | 11 | |
| α-helix | 137-139 | 3 | |
| α-helix | 143-156 | 14 | |
| α-helix | 176-198 | 23 | |
| α-helix | 206-213 | 8 | |
| α-helix | 217-228 | 12 | |
| α-helix | 235-237 | 3 | |
| α-helix | 238-243 | 6 | |
| α-helix | 244-251 | 8 | |
| α-helix | 256-269 | 14 | |
| α-helix | 272-274 | 3 | |
| α-helix | 279-287 | 9 | |
| α-helix | 296-302 | 7 | |
| α-helix | 304-311 | 8 | |
| α-helix | 324-338 | 15 | |
| α-helix | 345-361 | 17 | |
| α-helix | 366-382 | 17 | |
| α-helix | 393-408 | 16 | |
| α-helix | 413-416 | 4 | |
| α-helix | 421-424 | 4 | |
| α-helix | 430-446 | 17 | |
| α-helix | 454-468 | 15 | |
| α-helix | 485-497 | 13 | |
| α-helix | 503-520 | 18 | |
| α-helix | 525-543 | 19 | |
| α-helix | 553-573 | 21 | |
| α-helix | 578-594 | 17 | |
| α-helix | 600-616 | 17 | |
| α-helix | 621-636 | 16 | |
| α-helix | 643-659 | 17 | |
| α-helix | 663-675 | 13 | |
| α-helix | 697-707 | 11 | |
| α-helix | 713-731 | 19 | |
| α-helix | 741-753 | 13 | |
| α-helix | 763-776 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 12-18 | 7 | 1 |
| β-strand | 42 | 1 | 2 |
| β-strand | 49-56 | 8 | 1 |
| β-strand | 63-64 | 2 | 3 |
| β-strand | 68-78 | 11 | 4 |
| α-helix | 82-84 | 3 | |
| β-strand | 86-89 | 4 | 4 |
| β-strand | 92-96 | 5 | 4 |
| β-strand | 100-101 | 2 | 3 |
| β-strand | 106-110 | 5 | 1 |
| β-strand | 122 | 1 | 4 |
| β-strand | 126-136 | 11 | 4 |
| β-strand | 143-149 | 7 | 4 |
| β-strand | 151 | 1 | 2 |
| β-strand | 154 | 1 | 5 |
| β-strand | 164-166 | 3 | 6 |
| β-strand | 169-170 | 2 | 7 |
| β-strand | 174-175 | 2 | 7 |
| β-strand | 178-180 | 3 | 6 |
| β-strand | 184-186 | 3 | 8 |
| β-strand | 190-196 | 7 | 6 |
| β-strand | 199-200 | 2 | 7 |
| β-strand | 204 | 1 | 9 |
| β-strand | 209-219 | 11 | 10 |
| β-strand | 222-224 | 3 | 10 |
| β-strand | 231-232 | 2 | 10 |
| β-strand | 245-251 | 7 | 6 |
| β-strand | 264 | 1 | 10 |
| β-strand | 268-276 | 9 | 10 |
| β-strand | 278-279 | 2 | 11 |
| β-strand | 280 | 1 | 9 |
| β-strand | 285-286 | 2 | 11 |
| β-strand | 289-292 | 4 | 10 |
| β-strand | 293-295 | 3 | 8 |
| β-strand | 296 | 1 | 5 |
| α-helix | 297-298 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-6 | 4 | 12 |
| α-helix | 20-25 | 6 | |
| β-strand | 33-36 | 4 | 12 |
| α-helix | 43-52 | 10 | |
| β-strand | 55-58 | 4 | 12 |
| β-strand | 72-77 | 6 | 13 |
| β-strand | 80-85 | 6 | 13 |
| α-helix | 98-106 | 9 | |
| β-strand | 110-112 | 3 | 13 |
| β-strand | 120-124 | 5 | 13 |
| β-strand | 127-131 | 5 | 13 |
| β-strand | 149-151 | 3 | 12 |
| β-strand | 155 | 1 | 12 |
| β-strand | 159-168 | 10 | 12 |
| β-strand | 171-180 | 10 | 12 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Vacuolar protein sorting-associated protein 35 | A | protein | 796 | Mus musculus | Q9EQH3 (AlphaFold model) |
| Vacuolar protein sorting-associated protein 26A | B | protein | 327 | Mus musculus | P40336 (AlphaFold model) |
| Vacuolar protein sorting-associated protein 29 | C | protein | 182 | Mus musculus | Q9QZ88 (AlphaFold model) |
>6VAC_1 Vacuolar protein sorting-associated protein 35 (chains A) MPTTQQSPQDEQEKLLDEAIQAVKVQSFQMKRCLDKNKLMDALKHASNMLGELRTSMLSP KSYYELYMAISDELHYLEVYLTDEFAKGRKVADLYELVQYAGNIIPRLYLLITVGVVYVK SFPQSRKDILKDLVEMCRGVQHPLRGLFLRNYLLQCTRNILPDEGEPTDEETTGDISDSM DFVLLNFAEMNKLWVRMQHQGHSRDREKRERERQELRILVGTNLVRLSQLEGVNVERYKQ IVLTGILEQVVNCRDALAQEYLMECIIQVFPDEFHLQTLNPFLRACAELHQNVNVKNIII ALIDRLALFAHREDGPGIPAEIKLFDIFSQQVATVIQSRQDMPSEDVVSLQVSLINLAMK CYPDRVDYVDKVLETTVEIFNKLNLEHIATSSAVSKELTRLLKIPVDTYNNILTVLKLKH FHPLFEYFDYESRKSMSCYVLSNVLDYNTEIVSQDQVDSIMNLVSTLIQDQPDQPVEDPD PEDFADEQSLVGRFIHLLRSDDPDQQYLILNTARKHFGAGGNQRIRFTLPPLVFAAYQLA FRYKENSQMDDKWEKKCQKIFSFAHQTISALIKAELAELPLRLFLQGALAAGEIGFENHE TVAYEFMSQAFSLYEDEISDSKAQLAAITLIIGTFERMKCFSEENHEPLRTQCALAASKL LKKPDQGRAVSTCAHLFWSGRNTDKNGEELHGGKRVMECLKKALKIANQCMDPSLQVQLF IEILNRYIYFYEKENDAVTIQVLNQLIQKIREDLPNLESSEETEQINKHFHNTLEHLRSR RESPESEGPIYEGLIL
>6VAC_2 Vacuolar protein sorting-associated protein 26A (chains B) MSFLGGFFGPICEIDVALNDGETRKMAEMKTEDGKVEKHYLFYDGESVSGKVNLAFKQPG KRLEHQGIRIEFVGQIELFNDKSNTHEFVNLVKELALPGELTQSRSYDFEFMQVEKPYES YIGANVRLRYFLKVTIVRRLTDLVKEYDLIVHQLATYPDVNNSIKMEVGIEDCLHIEFEY NKSKYHLKDVIVGKIYFLLVRIKIQHMELQLIKKEITGIGPSTTTETETIAKYEIMDGAP VKGESIPIRLFLAGYDPTPTMRDVNKKFSVRYFLNLVLVDEEDRRYFKQQEIILWRKAPE KLRKQRTNFHQRFESPDSQASAEQPEM
>6VAC_3 Vacuolar protein sorting-associated protein 29 (chains C) MLVLVLGDLHIPHRCNSLPAKFKKLLVPGKIQHILCTGNLCTKESYDYLKTLAGDVHIVR GDFDENLNYPEQKVVTVGQFKIGLIHGHQVIPWGDMASLALLQRQFDVDILISGHTHKFE AFEHENKFYINPGSATGAYNALETNIIPSFVLMDIQASTVVTYVYQLIGDDVKVERIEYK KS
Mammalian Retromer Is an Adaptable Scaffold for Cargo Sorting from Endosomes. Kendall, A.K., Xie, B., Xu, P. et al. Structure (2020) 28:393-405.e4. DOI 10.1016/j.str.2020.01.009 · PubMed
Other PDB entries of the same protein (UniProt Q9EQH3 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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