Vps35/Vps29 arch of fungal membrane-assembled retromer:Grd19 complex. Determined by electron microscopy at 9.5 Å resolution. Released 10 Feb 2021.
Explore 7BLP in 3D Show helices and sheets RCSB PDB PDBe
7BLP contains 95 α-helices and 31 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 | 13-33 | 21 | |
| α-helix | 38-49 | 12 | |
| α-helix | 50-53 | 4 | |
| α-helix | 59-86 | 28 | |
| α-helix | 92-95 | 4 | |
| α-helix | 96-98 | 3 | |
| α-helix | 102-119 | 18 | |
| α-helix | 124-134 | 11 | |
| α-helix | 135-137 | 3 | |
| α-helix | 141-155 | 15 | |
| α-helix | 171-194 | 24 | |
| α-helix | 198-200 | 3 | |
| α-helix | 201-222 | 22 | |
| α-helix | 228-231 | 4 | |
| α-helix | 232-236 | 5 | |
| α-helix | 237-246 | 10 | |
| α-helix | 250-262 | 13 | |
| α-helix | 265-269 | 5 | |
| α-helix | 272-279 | 8 | |
| α-helix | 288-304 | 17 | |
| α-helix | 389-403 | 15 | |
| α-helix | 408-425 | 18 | |
| α-helix | 430-447 | 18 | |
| α-helix | 457-472 | 16 | |
| α-helix | 477-481 | 5 | |
| α-helix | 483-490 | 8 | |
| α-helix | 494-510 | 17 | |
| α-helix | 518-532 | 15 | |
| α-helix | 561-572 | 12 | |
| α-helix | 577-590 | 14 | |
| α-helix | 598-617 | 20 | |
| α-helix | 625-645 | 21 | |
| α-helix | 653-670 | 18 | |
| α-helix | 675-690 | 16 | |
| α-helix | 695-709 | 15 | |
| α-helix | 717-731 | 15 | |
| α-helix | 737-751 | 15 | |
| α-helix | 756-758 | 3 | |
| α-helix | 771-786 | 16 | |
| α-helix | 791-810 | 20 | |
| α-helix | 818-832 | 15 | |
| α-helix | 836-838 | 3 | |
| α-helix | 840-856 | 17 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 5-8 | 4 | 1 |
| α-helix | 22-27 | 6 | |
| β-strand | 30 | 1 | 2 |
| β-strand | 33 | 1 | 2 |
| β-strand | 35-38 | 4 | 1 |
| α-helix | 45-54 | 10 | |
| β-strand | 57-60 | 4 | 1 |
| β-strand | 76-80 | 5 | 3 |
| β-strand | 83-87 | 5 | 3 |
| α-helix | 98-108 | 11 | |
| β-strand | 112-114 | 3 | 3 |
| β-strand | 122-127 | 6 | 3 |
| β-strand | 130-135 | 6 | 3 |
| β-strand | 137 | 1 | 4 |
| β-strand | 155 | 1 | 4 |
| β-strand | 156-163 | 8 | 1 |
| β-strand | 166-175 | 10 | 1 |
| β-strand | 183-192 | 10 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 13-33 | 21 | |
| α-helix | 38-49 | 12 | |
| α-helix | 50-53 | 4 | |
| α-helix | 59-86 | 28 | |
| α-helix | 92-95 | 4 | |
| α-helix | 96-98 | 3 | |
| α-helix | 102-119 | 18 | |
| α-helix | 124-134 | 11 | |
| α-helix | 141-154 | 14 | |
| α-helix | 171-194 | 24 | |
| α-helix | 198-200 | 3 | |
| α-helix | 201-223 | 23 | |
| α-helix | 228-231 | 4 | |
| α-helix | 232-236 | 5 | |
| α-helix | 237-246 | 10 | |
| α-helix | 250-262 | 13 | |
| α-helix | 265-269 | 5 | |
| α-helix | 272-279 | 8 | |
| α-helix | 288-304 | 17 | |
| 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 | 450-451 | 2 | |
| α-helix | 457-472 | 16 | |
| α-helix | 476-479 | 4 | |
| α-helix | 483-485 | 3 | |
| α-helix | 487-491 | 5 | |
| α-helix | 494-510 | 17 | |
| α-helix | 512-513 | 2 | |
| α-helix | 518-532 | 15 | |
| α-helix | 562-572 | 11 | |
| α-helix | 577-589 | 13 | |
| α-helix | 598-617 | 20 | |
| α-helix | 626-646 | 21 | |
| α-helix | 653-670 | 18 | |
| α-helix | 675-691 | 17 | |
| α-helix | 695-709 | 15 | |
| α-helix | 717-731 | 15 | |
| α-helix | 737-751 | 15 | |
| β-strand | 752 | 1 | 5 |
| β-strand | 754 | 1 | 5 |
| α-helix | 756-758 | 3 | |
| α-helix | 771-786 | 16 | |
| α-helix | 792-810 | 19 | |
| α-helix | 818-834 | 17 | |
| α-helix | 840-856 | 17 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-7 | 4 | 6 |
| β-strand | 13 | 1 | 7 |
| α-helix | 22-27 | 6 | |
| β-strand | 35-38 | 4 | 6 |
| β-strand | 43 | 1 | 7 |
| α-helix | 45-54 | 10 | |
| β-strand | 57-60 | 4 | 6 |
| β-strand | 79-80 | 2 | 8 |
| β-strand | 83-84 | 2 | 8 |
| β-strand | 85-87 | 3 | 9 |
| α-helix | 99-108 | 10 | |
| β-strand | 112-114 | 3 | 9 |
| β-strand | 123-127 | 5 | 9 |
| β-strand | 130-134 | 5 | 9 |
| β-strand | 156-163 | 8 | 6 |
| β-strand | 166-176 | 11 | 6 |
| β-strand | 182-192 | 11 | 6 |
| 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) |
>7BLP_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
>7BLP_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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