Vps35/Vps29 arch of fungal membrane-assembled retromer:Vps5 (SNX-BAR) complex. Determined by electron microscopy at 9.3 Å resolution. Released 10 Feb 2021.
Explore 7BLR in 3D Show helices and sheets RCSB PDB PDBe
7BLR contains 95 α-helices and 35 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 | 13-32 | 20 | |
| α-helix | 38-53 | 16 | |
| α-helix | 59-83 | 25 | |
| α-helix | 92-95 | 4 | |
| α-helix | 103-119 | 17 | |
| α-helix | 124-134 | 11 | |
| α-helix | 135-137 | 3 | |
| α-helix | 141-155 | 15 | |
| α-helix | 171-191 | 21 | |
| α-helix | 198-200 | 3 | |
| α-helix | 201-222 | 22 | |
| α-helix | 228-236 | 9 | |
| α-helix | 238-246 | 9 | |
| α-helix | 249-262 | 14 | |
| α-helix | 266-279 | 14 | |
| α-helix | 288-303 | 16 | |
| α-helix | 389-403 | 15 | |
| α-helix | 408-425 | 18 | |
| α-helix | 430-435 | 6 | |
| α-helix | 436-442 | 7 | |
| α-helix | 443-447 | 5 | |
| α-helix | 458-470 | 13 | |
| α-helix | 477-480 | 4 | |
| α-helix | 483-486 | 4 | |
| α-helix | 487-491 | 5 | |
| α-helix | 494-510 | 17 | |
| α-helix | 519-531 | 13 | |
| α-helix | 561-572 | 12 | |
| α-helix | 577-590 | 14 | |
| α-helix | 598-600 | 3 | |
| α-helix | 602-617 | 16 | |
| α-helix | 620-622 | 3 | |
| α-helix | 626-645 | 20 | |
| α-helix | 654-670 | 17 | |
| α-helix | 677-690 | 14 | |
| α-helix | 695-710 | 16 | |
| α-helix | 720-732 | 13 | |
| α-helix | 737-746 | 10 | |
| β-strand | 752 | 1 | 1 |
| β-strand | 760 | 1 | 2 |
| β-strand | 766 | 1 | 2 |
| β-strand | 769 | 1 | 1 |
| α-helix | 772-785 | 14 | |
| α-helix | 791-810 | 20 | |
| α-helix | 818-835 | 18 | |
| α-helix | 840-855 | 16 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-5 | 2 | 3 |
| β-strand | 13 | 1 | 4 |
| α-helix | 22-26 | 5 | |
| β-strand | 43 | 1 | 4 |
| α-helix | 45-54 | 10 | |
| β-strand | 78 | 1 | 5 |
| β-strand | 85-87 | 3 | 5 |
| α-helix | 98-108 | 11 | |
| β-strand | 112-114 | 3 | 5 |
| β-strand | 122-123 | 2 | 6 |
| β-strand | 126-127 | 2 | 7 |
| β-strand | 130-131 | 2 | 7 |
| β-strand | 133 | 1 | 5 |
| β-strand | 134-135 | 2 | 6 |
| β-strand | 157-163 | 7 | 3 |
| β-strand | 166-176 | 11 | 3 |
| β-strand | 182-192 | 11 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 13-33 | 21 | |
| α-helix | 38-52 | 15 | |
| α-helix | 59-83 | 25 | |
| α-helix | 84-86 | 3 | |
| α-helix | 92-95 | 4 | |
| α-helix | 102-119 | 18 | |
| α-helix | 124-134 | 11 | |
| α-helix | 135-137 | 3 | |
| α-helix | 141-155 | 15 | |
| α-helix | 156-158 | 3 | |
| α-helix | 171-191 | 21 | |
| α-helix | 201-222 | 22 | |
| α-helix | 228-234 | 7 | |
| α-helix | 236-246 | 11 | |
| α-helix | 249-250 | 2 | |
| α-helix | 251-255 | 5 | |
| α-helix | 256-262 | 7 | |
| α-helix | 267-269 | 3 | |
| α-helix | 273-279 | 7 | |
| α-helix | 288-303 | 16 | |
| α-helix | 389-403 | 15 | |
| α-helix | 408-425 | 18 | |
| α-helix | 431-434 | 4 | |
| α-helix | 435-442 | 8 | |
| α-helix | 443-447 | 5 | |
| α-helix | 457-472 | 16 | |
| α-helix | 477-480 | 4 | |
| α-helix | 485-491 | 7 | |
| α-helix | 494-509 | 16 | |
| α-helix | 518-531 | 14 | |
| α-helix | 562-574 | 13 | |
| α-helix | 580-590 | 11 | |
| α-helix | 602-617 | 16 | |
| α-helix | 625-645 | 21 | |
| α-helix | 655-670 | 16 | |
| α-helix | 674-691 | 18 | |
| α-helix | 695-710 | 16 | |
| α-helix | 717-732 | 16 | |
| α-helix | 737-747 | 11 | |
| α-helix | 748-750 | 3 | |
| α-helix | 756-758 | 3 | |
| β-strand | 759 | 1 | 8 |
| α-helix | 761-763 | 3 | |
| β-strand | 767 | 1 | 8 |
| α-helix | 771-785 | 15 | |
| α-helix | 791-810 | 20 | |
| α-helix | 818-834 | 17 | |
| α-helix | 836-837 | 2 | |
| α-helix | 840-855 | 16 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 5 | 1 | 9 |
| α-helix | 22-27 | 6 | |
| α-helix | 45-54 | 10 | |
| β-strand | 76-80 | 5 | 10 |
| β-strand | 83-87 | 5 | 10 |
| α-helix | 98-108 | 11 | |
| β-strand | 126-127 | 2 | 11 |
| β-strand | 130-131 | 2 | 11 |
| β-strand | 137 | 1 | 12 |
| β-strand | 155 | 1 | 12 |
| β-strand | 157-158 | 2 | 13 |
| β-strand | 160 | 1 | 9 |
| β-strand | 162-163 | 2 | 14 |
| β-strand | 166-167 | 2 | 14 |
| β-strand | 171-172 | 2 | 13 |
| β-strand | 174-175 | 2 | 15 |
| β-strand | 183-184 | 2 | 15 |
| β-strand | 191-192 | 2 | 14 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Vacuolar protein sorting-associated protein 35 | A, C | protein | 869 | Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719) | G0S709 (AlphaFold model) |
| Vacuolar protein sorting-associated protein 29 | B, D | protein | 202 | Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719) | G0RZB5 (AlphaFold model) |
>7BLR_1 Vacuolar protein sorting-associated protein 35 (chains A, C) MSTPAPPEEQARLLEDALIAVRQQTAMMRKFLDTPGKLMDALKCCSTLVSELRTSSLSPK QYYELYMAVFDALRYLSAHLRENHPVNHLADLYELVQYAGNIIPRLYLMITVGTAYMSID GAPVKELMKDMMDMSRGVQHPVRGLFLRYYLSGQARDYLPTGDSDGPEGNLQDSINFILT NFVEMNKLWVRLQHQGHSRERDLRTQERRELQLLVGSNIVRLSQLVDLPTYRDSILGPLL EQIVQCRDILAQEYLLEVITQVFPDEYHLHTLDQFLGAVSRLNPHVNVKAIVIGMMNRLS DYAERESQNEPEEDRAKLEEEALAKLLEKTKLGQNSELEPQNGDHPDTEVSSTTDSAQAP STADSDTTAVNGEEEPVRKRRGIPVNVPLYDIFFDQVQHLVQAQHLPIQDTIALCCSLAN LSLNIYPERLDYVDGILAYALAKVKEHANSADLHSQPAQQSLLSLLQSPLRRYVSIFTAL SLPTYVSLFQAQTYPTRRAIAGEIVRTLLKNQTLISTPAHLENVLEILKVLIKEGSQPPA GYPGVVQPRARPLETDETMEEQGWLARLVHLIHSDDNDTQFRLLQMTRKAYAEGNERIRT TTPPLITAGLKLARRFKAREHYDDNWSSQSSSLFKFLHSAISTLYTRVNGPGVADLCLRL FCSCGQVADMTEFEEVAYEFFAQAFTVYEESISDSKAQFQAVCVIASALHRTRNFGRENY DTLITKCAQHASKLLRKPDQCRAVYLASHLWWATPIAARGETEDTELYRDGKRVLECLQR ALRVADSCMETATSIELFVEILDRYVYYFDQRNESVTTKYLNGLIELIHSNLAGNQQDSA SVEASRKHFIQTLEMIQSKEFEGIVVAPK
>7BLR_2 Vacuolar protein sorting-associated protein 29 (chains B, D) SMAFLILVIGNLHIPDRALDIPPKFKKLLSPGKISQTLCLGNLTDRATYDYLRSISPDLK IVRGRMDVEATSLPLMQVVTHGSLRIGFLEGFTLVSEEPDVLLAEANKLDVDVLCWAGGS HRFECFEYMDKFFVNPGSATGAFTTDWLAEGEEVVPSFCLMDVQGISLTLYVYQLRKDEN GTENVAVEKVTYTKPVEPTGAS
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 G0S709 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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