VPS35/VPS29 arch of metazoan membrane-assembled retromer:SNX3 complex modelled with human proteins. Determined by electron microscopy at 8.9 Å resolution. Released 10 Feb 2021.
Explore 7BLN in 3D Show helices and sheets RCSB PDB PDBe
7BLN contains 93 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 | 14-35 | 22 | |
| α-helix | 39-52 | 14 | |
| α-helix | 60-86 | 27 | |
| 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 | |
| α-helix | 143-160 | 18 | |
| α-helix | 176-199 | 24 | |
| α-helix | 203-205 | 3 | |
| α-helix | 206-229 | 24 | |
| α-helix | 235-237 | 3 | |
| α-helix | 238-242 | 5 | |
| α-helix | 243-252 | 10 | |
| α-helix | 257-269 | 13 | |
| α-helix | 272-287 | 16 | |
| α-helix | 296-310 | 15 | |
| α-helix | 324-338 | 15 | |
| α-helix | 344-361 | 18 | |
| α-helix | 366-382 | 17 | |
| α-helix | 386-387 | 2 | |
| β-strand | 388 | 1 | 7 |
| α-helix | 389 | 1 | |
| α-helix | 393-403 | 11 | |
| α-helix | 404-408 | 5 | |
| α-helix | 413-416 | 4 | |
| α-helix | 419-421 | 3 | |
| α-helix | 423-427 | 5 | |
| β-strand | 428 | 1 | 7 |
| α-helix | 430-446 | 17 | |
| α-helix | 454-468 | 15 | |
| α-helix | 488-498 | 11 | |
| α-helix | 503-518 | 16 | |
| α-helix | 525-545 | 21 | |
| α-helix | 553-573 | 21 | |
| α-helix | 578-594 | 17 | |
| α-helix | 599-616 | 18 | |
| α-helix | 621-636 | 16 | |
| α-helix | 643-657 | 15 | |
| α-helix | 663-672 | 10 | |
| α-helix | 674-678 | 5 | |
| β-strand | 681 | 1 | 8 |
| β-strand | 689 | 1 | 8 |
| α-helix | 693-707 | 15 | |
| α-helix | 713-731 | 19 | |
| α-helix | 740-751 | 12 | |
| α-helix | 761-775 | 15 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-6 | 5 | 1 |
| β-strand | 11 | 1 | 2 |
| α-helix | 20-25 | 6 | |
| β-strand | 33-36 | 4 | 1 |
| β-strand | 41 | 1 | 2 |
| α-helix | 43-52 | 10 | |
| β-strand | 56-58 | 3 | 1 |
| β-strand | 72-77 | 6 | 3 |
| β-strand | 80-85 | 6 | 3 |
| α-helix | 96-106 | 11 | |
| β-strand | 110-112 | 3 | 3 |
| β-strand | 120-124 | 5 | 3 |
| β-strand | 127-131 | 5 | 3 |
| β-strand | 149-155 | 7 | 1 |
| β-strand | 160-166 | 7 | 1 |
| β-strand | 173-179 | 7 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 14-35 | 22 | |
| α-helix | 39-52 | 14 | |
| α-helix | 60-86 | 27 | |
| 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 | |
| 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 | 243-253 | 11 | |
| α-helix | 257-269 | 13 | |
| α-helix | 272-277 | 6 | |
| α-helix | 279-287 | 9 | |
| α-helix | 295-310 | 16 | |
| α-helix | 324-338 | 15 | |
| α-helix | 344-361 | 18 | |
| α-helix | 366-382 | 17 | |
| α-helix | 385-386 | 2 | |
| β-strand | 388 | 1 | 9 |
| α-helix | 393-408 | 16 | |
| α-helix | 413-416 | 4 | |
| α-helix | 419-427 | 9 | |
| β-strand | 428 | 1 | 9 |
| α-helix | 430-446 | 17 | |
| α-helix | 454-468 | 15 | |
| α-helix | 485-487 | 3 | |
| α-helix | 488-498 | 11 | |
| α-helix | 503-518 | 16 | |
| α-helix | 525-545 | 21 | |
| α-helix | 553-573 | 21 | |
| α-helix | 578-594 | 17 | |
| α-helix | 599-616 | 18 | |
| α-helix | 621-637 | 17 | |
| α-helix | 643-657 | 15 | |
| α-helix | 663-672 | 10 | |
| α-helix | 674-678 | 5 | |
| α-helix | 693-710 | 18 | |
| α-helix | 713-731 | 19 | |
| α-helix | 740-751 | 12 | |
| α-helix | 761-777 | 17 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Vacuolar protein sorting-associated protein 29 | B, D | protein | 182 | Homo sapiens | Q9UBQ0 (AlphaFold model) |
| Vacuolar protein sorting-associated protein 35 | A, C | protein | 796 | Homo sapiens | Q96QK1 (AlphaFold model) |
>7BLN_1 Vacuolar protein sorting-associated protein 29 (chains B, D) MLVLVLGDLHIPHRCNSLPAKFKKLLVPGKIQHILCTGNLCTKESYDYLKTLAGDVHIVR GDFDENLNYPEQKVVTVGQFKIGLIHGHQVIPWGDMASLALLQRQFDVDILISGHTHKFE AFEHENKFYINPGSATGAYNALETNIIPSFVLMDIQASTVVTYVYQLIGDDVKVERIEYK KP
>7BLN_2 Vacuolar protein sorting-associated protein 35 (chains A, C) MPTTQQSPQDEQEKLLDEAIQAVKVQSFQMKRCLDKNKLMDALKHASNMLGELRTSMLSP KSYYELYMAISDELHYLEVYLTDEFAKGRKVADLYELVQYAGNIIPRLYLLITVGVVYVK SFPQSRKDILKDLVEMCRGVQHPLRGLFLRNYLLQCTRNILPDEGEPTDEETTGDISDSM DFVLLNFAEMNKLWVRMQHQGHSRDREKRERERQELRILVGTNLVRLSQLEGVNVERYKQ IVLTGILEQVVNCRDALAQEYLMECIIQVFPDEFHLQTLNPFLRACAELHQNVNVKNIII ALIDRLALFAHREDGPGIPADIKLFDIFSQQVATVIQSRQDMPSEDVVSLQVSLINLAMK CYPDRVDYVDKVLETTVEIFNKLNLEHIATSSAVSKELTRLLKIPVDTYNNILTVLKLKH FHPLFEYFDYESRKSMSCYVLSNVLDYNTEIVSQDQVDSIMNLVSTLIQDQPDQPVEDPD PEDFADEQSLVGRFIHLLRSEDPDQQYLILNTARKHFGAGGNQRIRFTLPPLVFAAYQLA FRYKENSKVDDKWEKKCQKIFSFAHQTISALIKAELAELPLRLFLQGALAAGEIGFENHE TVAYEFMSQAFSLYEDEISDSKAQLAAITLIIGTFERMKCFSEENHEPLRTQCALAASKL LKKPDQGRAVSTCAHLFWSGRNTDKNGEELHGGKRVMECLKKALKIANQCMDPSLQVQLF IEILNRYIYFYEKENDAVTIQVLNQLIQKIREDLPNLESSEETEQINKHFHNTLEHLRLR RESPESEGPIYEGLIL
Architecture and mechanism of metazoan retromer:SNX3 tubular coat assembly. Leneva, N., Kovtun, O., Morado, D.R. et al. Sci Adv (2021) 7. DOI 10.1126/sciadv.abf8598 · PubMed
Other PDB entries of the same protein (UniProt Q9UBQ0 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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