Structure of retromer VPS29-VPS35 (483-796) complexed with Fam21A repeat 20 (1289-1302). Determined by X-ray diffraction at 3.01 Å resolution. Released 21 Aug 2024.
Explore 8TTC in 3D Show helices and sheets RCSB PDB PDBe
8TTC contains 36 α-helices and 30 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 |
|---|---|---|---|
| β-strand | 2-6 | 5 | 1 |
| α-helix | 20-25 | 6 | |
| β-strand | 33-36 | 4 | 1 |
| α-helix | 43-52 | 10 | |
| β-strand | 55-58 | 4 | 1 |
| β-strand | 72-77 | 6 | 2 |
| β-strand | 79-85 | 7 | 2 |
| α-helix | 96-106 | 11 | |
| β-strand | 110-112 | 3 | 2 |
| β-strand | 120-124 | 5 | 2 |
| β-strand | 127-131 | 5 | 2 |
| β-strand | 140 | 1 | 3 |
| β-strand | 143 | 1 | 3 |
| β-strand | 149-155 | 7 | 1 |
| β-strand | 159-168 | 10 | 1 |
| β-strand | 171-180 | 10 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 503-518 | 16 | |
| α-helix | 521-545 | 25 | |
| α-helix | 553-573 | 21 | |
| α-helix | 578-594 | 17 | |
| α-helix | 599-617 | 19 | |
| α-helix | 621-637 | 17 | |
| α-helix | 643-658 | 16 | |
| α-helix | 663-673 | 11 | |
| α-helix | 676-679 | 4 | |
| β-strand | 681 | 1 | 4 |
| α-helix | 683-685 | 3 | |
| β-strand | 689 | 1 | 4 |
| α-helix | 693-708 | 16 | |
| α-helix | 713-732 | 20 | |
| α-helix | 740-753 | 14 | |
| α-helix | 754-756 | 3 | |
| α-helix | 761-778 | 18 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-6 | 4 | 5 |
| α-helix | 20-25 | 6 | |
| β-strand | 33-36 | 4 | 5 |
| α-helix | 43-52 | 10 | |
| β-strand | 56-58 | 3 | 5 |
| β-strand | 72-77 | 6 | 6 |
| β-strand | 80-85 | 6 | 6 |
| α-helix | 96-106 | 11 | |
| β-strand | 110-112 | 3 | 6 |
| β-strand | 120-124 | 5 | 6 |
| β-strand | 127-131 | 5 | 6 |
| β-strand | 140 | 1 | 7 |
| β-strand | 143 | 1 | 7 |
| β-strand | 149-155 | 7 | 5 |
| β-strand | 159-168 | 10 | 5 |
| β-strand | 171-180 | 10 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 497-499 | 3 | |
| α-helix | 503-518 | 16 | |
| α-helix | 525-545 | 21 | |
| α-helix | 553-572 | 20 | |
| α-helix | 578-594 | 17 | |
| α-helix | 599-617 | 19 | |
| α-helix | 621-637 | 17 | |
| α-helix | 643-658 | 16 | |
| α-helix | 663-672 | 10 | |
| α-helix | 674-678 | 5 | |
| β-strand | 681 | 1 | 8 |
| α-helix | 683-685 | 3 | |
| β-strand | 689 | 1 | 8 |
| α-helix | 693-708 | 16 | |
| α-helix | 713-731 | 19 | |
| α-helix | 740-753 | 14 | |
| α-helix | 761-778 | 18 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Vacuolar protein sorting-associated protein 29 | A, C | protein | 182 | Mus musculus | Q9QZ88 (AlphaFold model) |
| Vacuolar protein sorting-associated protein 35 | B, D | protein | 316 | Mus musculus | Q9EQH3 (AlphaFold model) |
| Ser-ile-phe-asp-asp-asp-met-asp-asp-ile-phe-ser-ser-gly | E | protein | 14 | Homo sapiens | Q641Q2 (AlphaFold model) |
>8TTC_1 Vacuolar protein sorting-associated protein 29 (chains A, C) MLVLVLGDLHIPHRCNSLPAKFKKLLVPGKIQHILCTGNLCTKESYDYLKTLAGDVHIVR GDFDENLNYPEQKVVTVGQFKIGLIHGHQVIPWGDMASLALLQRQFDVDILISGHTHKFE AFEHENKFYINPGSATGAYNALETNIIPSFVLMDIQASTVVTYVYQLIGDDVKVERIEYK KS
>8TTC_2 Vacuolar protein sorting-associated protein 35 (chains B, D) GSDFADEQSLVGRFIHLLRSDDPDQQYLILNTARKHFGAGGNQRIRFTLPPLVFAAYQLA FRYKENSQMDDKWEKKCQKIFSFAHQTISALIKAELAELPLRLFLQGALAAGEIGFENHE TVAYEFMSQAFSLYEDEISDSKAQLAAITLIIGTFERMKCFSEENHEPLRTQCALAASKL LKKPDQGRAVSTCAHLFWSGRNTDKNGEELHGGKRVMECLKKALKIANQCMDPSLQVQLF IEILNRYIYFYEKENDAVTIQVLNQLIQKIREDLPNLESSEETEQINKHFHNTLEHLRSR RESPESEGPIYEGLIL
>8TTC_3 SER-ILE-PHE-ASP-ASP-ASP-MET-ASP-ASP-ILE-PHE-SER-SER-GLY (chains E) SIFDDDMDDIFSSG
| ID | Name | Formula | Copies |
|---|---|---|---|
| CIT | Citric acid | C6 H8 O7 | 2 |
Water and common crystallization additives (PEG, GOL, ACT) are not listed.
Structural basis for coupling of the WASH subunit FAM21 with the endosomal SNX27-Retromer complex. Guo, Q., Chen, K.E., Gimenez-Andres, M. et al. Proc Natl Acad Sci U S A (2024) 121:e2405041121-e2405041121. DOI 10.1073/pnas.2405041121 · PubMed
Other PDB entries of the same protein (UniProt Q9QZ88 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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