Mouse retromer (VPS26/VPS35/VPS29) heterotrimers. Determined by electron microscopy at 4.9 Å resolution. Released 12 Oct 2022.
Explore 7U6F in 3D Show helices and sheets RCSB PDB PDBe
7U6F contains 49 α-helices and 34 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 |
|---|---|---|---|
| β-strand | 12-18 | 7 | 1 |
| β-strand | 29-30 | 2 | 2 |
| α-helix | 32-34 | 3 | |
| β-strand | 36-37 | 2 | 2 |
| β-strand | 40-42 | 3 | 3 |
| β-strand | 46-56 | 11 | 1 |
| β-strand | 63-78 | 16 | 3 |
| β-strand | 86-101 | 16 | 3 |
| β-strand | 105-114 | 10 | 1 |
| β-strand | 122 | 1 | 3 |
| β-strand | 126-136 | 11 | 3 |
| β-strand | 143-151 | 9 | 3 |
| β-strand | 164-170 | 7 | 4 |
| β-strand | 174-180 | 7 | 4 |
| β-strand | 184-186 | 3 | 5 |
| β-strand | 190-200 | 11 | 4 |
| β-strand | 204-217 | 14 | 6 |
| β-strand | 224-237 | 14 | 6 |
| β-strand | 245-251 | 7 | 4 |
| α-helix | 252-255 | 4 | |
| β-strand | 264 | 1 | 6 |
| β-strand | 268-280 | 13 | 6 |
| β-strand | 285-286 | 2 | 6 |
| β-strand | 289-292 | 4 | 6 |
| β-strand | 293-295 | 3 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-5 | 3 | 7 |
| α-helix | 22-25 | 4 | |
| β-strand | 33-35 | 3 | 7 |
| α-helix | 43-52 | 10 | |
| β-strand | 56-57 | 2 | 7 |
| β-strand | 73-77 | 5 | 8 |
| β-strand | 80-84 | 5 | 8 |
| α-helix | 96-106 | 11 | |
| β-strand | 110-112 | 3 | 8 |
| β-strand | 120-124 | 5 | 8 |
| β-strand | 127-131 | 5 | 8 |
| β-strand | 149-155 | 7 | 7 |
| β-strand | 159-168 | 10 | 7 |
| β-strand | 171-180 | 10 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 14-35 | 22 | |
| α-helix | 39-50 | 12 | |
| α-helix | 60-86 | 27 | |
| α-helix | 94-97 | 4 | |
| α-helix | 98-100 | 3 | |
| α-helix | 104-121 | 18 | |
| α-helix | 123-125 | 3 | |
| α-helix | 126-136 | 11 | |
| α-helix | 137-139 | 3 | |
| α-helix | 143-156 | 14 | |
| α-helix | 176-196 | 21 | |
| α-helix | 203-205 | 3 | |
| α-helix | 206-229 | 24 | |
| α-helix | 235-237 | 3 | |
| α-helix | 238-242 | 5 | |
| α-helix | 243-251 | 9 | |
| α-helix | 256-269 | 14 | |
| α-helix | 273-275 | 3 | |
| α-helix | 279-287 | 9 | |
| α-helix | 295-310 | 16 | |
| α-helix | 324-338 | 15 | |
| α-helix | 344-360 | 17 | |
| α-helix | 367-382 | 16 | |
| α-helix | 393-408 | 16 | |
| α-helix | 413-416 | 4 | |
| α-helix | 421-424 | 4 | |
| α-helix | 425-427 | 3 | |
| α-helix | 430-446 | 17 | |
| α-helix | 454-467 | 14 | |
| α-helix | 485-497 | 13 | |
| α-helix | 505-512 | 8 | |
| α-helix | 513-517 | 5 | |
| α-helix | 518-519 | 2 | |
| α-helix | 525-545 | 21 | |
| α-helix | 553-573 | 21 | |
| α-helix | 579-594 | 16 | |
| α-helix | 629-637 | 9 | |
| α-helix | 646-658 | 13 | |
| α-helix | 663-673 | 11 | |
| α-helix | 674-677 | 4 | |
| α-helix | 696-706 | 11 | |
| α-helix | 713-731 | 19 | |
| α-helix | 741-753 | 13 | |
| α-helix | 763-777 | 15 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Vacuolar protein sorting-associated protein 35 | D1 | protein | 796 | Mus musculus | Q9EQH3 (AlphaFold model) |
| Vacuolar protein sorting-associated protein 26A | B3 | protein | 327 | Mus musculus | P40336 (AlphaFold model) |
| Vacuolar protein sorting-associated protein 29 | B4 | protein | 182 | Mus musculus | Q9QZ88 (AlphaFold model) |
>7U6F_1 Vacuolar protein sorting-associated protein 35 (chains D1) MPTTQQSPQDEQEKLLDEAIQAVKVQSFQMKRCLDKNKLMDALKHASNMLGELRTSMLSP KSYYELYMAISDELHYLEVYLTDEFAKGRKVADLYELVQYAGNIIPRLYLLITVGVVYVK SFPQSRKDILKDLVEMCRGVQHPLRGLFLRNYLLQCTRNILPDEGEPTDEETTGDISDSM DFVLLNFAEMNKLWVRMQHQGHSRDREKRERERQELRILVGTNLVRLSQLEGVNVERYKQ IVLTGILEQVVNCRDALAQEYLMECIIQVFPDEFHLQTLNPFLRACAELHQNVNVKNIII ALIDRLALFAHREDGPGIPAEIKLFDIFSQQVATVIQSRQDMPSEDVVSLQVSLINLAMK CYPDRVDYVDKVLETTVEIFNKLNLEHIATSSAVSKELTRLLKIPVDTYNNILTVLKLKH FHPLFEYFDYESRKSMSCYVLSNVLDYNTEIVSQDQVDSIMNLVSTLIQDQPDQPVEDPD PEDFADEQSLVGRFIHLLRSDDPDQQYLILNTARKHFGAGGNQRIRFTLPPLVFAAYQLA FRYKENSQMDDKWEKKCQKIFSFAHQTISALIKAELAELPLRLFLQGALAAGEIGFENHE TVAYEFMSQAFSLYEDEISDSKAQLAAITLIIGTFERMKCFSEENHEPLRTQCALAASKL LKKPDQGRAVSTCAHLFWSGRNTDKNGEELHGGKRVMECLKKALKIANQCMDPSLQVQLF IEILNRYIYFYEKENDAVTIQVLNQLIQKIREDLPNLESSEETEQINKHFHNTLEHLRSR RESPESEGPIYEGLIL
>7U6F_2 Vacuolar protein sorting-associated protein 26A (chains B3) MSFLGGFFGPICEIDVALNDGETRKMAEMKTEDGKVEKHYLFYDGESVSGKVNLAFKQPG KRLEHQGIRIEFVGQIELFNDKSNTHEFVNLVKELALPGELTQSRSYDFEFMQVEKPYES YIGANVRLRYFLKVTIVRRLTDLVKEYDLIVHQLATYPDVNNSIKMEVGIEDCLHIEFEY NKSKYHLKDVIVGKIYFLLVRIKIQHMELQLIKKEITGIGPSTTTETETIAKYEIMDGAP VKGESIPIRLFLAGYDPTPTMRDVNKKFSVRYFLNLVLVDEEDRRYFKQQEIILWRKAPE KLRKQRTNFHQRFESPDSQASAEQPEM
>7U6F_3 Vacuolar protein sorting-associated protein 29 (chains B4) MLVLVLGDLHIPHRCNSLPAKFKKLLVPGKIQHILCTGNLCTKESYDYLKTLAGDVHIVR GDFDENLNYPEQKVVTVGQFKIGLIHGHQVIPWGDMASLALLQRQFDVDILISGHTHKFE AFEHENKFYINPGSATGAYNALETNIIPSFVLMDIQASTVVTYVYQLIGDDVKVERIEYK KS
Improved mammalian retromer cryo-EM structures reveal a new assembly interface. Kendall, A.K., Chandra, M., Xie, B. et al. J Biol Chem (2022) 298:102523-102523. DOI 10.1016/j.jbc.2022.102523 · 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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