Crystal structure of RidL(1-200) complexed with VPS29. Determined by X-ray diffraction at 2.46 Å resolution. Released 24 Jan 2018.
Explore 5WYH in 3D Show helices and sheets RCSB PDB PDBe
5WYH contains 26 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 |
|---|---|---|---|
| β-strand | 1-6 | 6 | 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 | 55-58 | 4 | 1 |
| β-strand | 72-77 | 6 | 3 |
| β-strand | 80-85 | 6 | 3 |
| α-helix | 96-106 | 11 | |
| β-strand | 110-113 | 4 | 3 |
| β-strand | 120-124 | 5 | 3 |
| β-strand | 127-131 | 5 | 3 |
| β-strand | 149-156 | 8 | 1 |
| β-strand | 159-168 | 10 | 1 |
| β-strand | 171-180 | 10 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 12-26 | 15 | |
| α-helix | 30-45 | 16 | |
| α-helix | 51-60 | 10 | |
| α-helix | 62-68 | 7 | |
| α-helix | 85-89 | 5 | |
| α-helix | 104-120 | 17 | |
| α-helix | 125-133 | 9 | |
| α-helix | 136-145 | 10 | |
| α-helix | 161-164 | 4 | |
| β-strand | 165-166 | 2 | 4 |
| β-strand | 174-175 | 2 | 4 |
| α-helix | 184-199 | 16 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 1-6 | 6 | 5 |
| β-strand | 11 | 1 | 6 |
| α-helix | 20-25 | 6 | |
| β-strand | 33-36 | 4 | 5 |
| β-strand | 41 | 1 | 6 |
| α-helix | 43-52 | 10 | |
| β-strand | 55-58 | 4 | 5 |
| β-strand | 66 | 1 | 3 |
| β-strand | 72-77 | 6 | 7 |
| β-strand | 80-85 | 6 | 7 |
| α-helix | 96-106 | 11 | |
| β-strand | 110-113 | 4 | 7 |
| β-strand | 120-124 | 5 | 7 |
| β-strand | 127-131 | 5 | 7 |
| β-strand | 149-156 | 8 | 5 |
| β-strand | 159-168 | 10 | 5 |
| β-strand | 171-180 | 10 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 12-26 | 15 | |
| α-helix | 30-45 | 16 | |
| α-helix | 51-60 | 10 | |
| α-helix | 62-68 | 7 | |
| α-helix | 85-89 | 5 | |
| α-helix | 104-120 | 17 | |
| α-helix | 125-133 | 9 | |
| α-helix | 136-145 | 10 | |
| α-helix | 161-164 | 4 | |
| β-strand | 165-166 | 2 | 8 |
| β-strand | 174-175 | 2 | 8 |
| α-helix | 184-198 | 15 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Vacuolar protein sorting-associated protein 29 | A, C | protein | 185 | Homo sapiens | Q9UBQ0 (AlphaFold model) |
| Interaptin | B, D | protein | 198 | Legionella pneumophila subsp. pneumophila ATCC 43290 | A0ABF7PFW6 (AlphaFold model) |
>5WYH_1 Vacuolar protein sorting-associated protein 29 (chains A, C) AGHRLVLVLGDLHIPHRCNSLPAKFKKLLVPGKIQHILCTGNLCTKESYDYLKTLAGDVH IVRGDFDENLNYPEQKVVTVGQFKIGLIHGHQVIPWGDMASLALLQRQFDVDILISGHTH KFEAFEHENKFYINPGSATGAYNALETNIIPSFVLMDIQASTVVTYVYQLIGDDVKVERI EYKKP
>5WYH_2 Interaptin (chains B, D) LEEYIRMAKNKEFFDALEEIAESAKNDETLRNELAKVLDDILKTDPSDPEAFRKIVAEHQ EFWDEHDPSLMEFNEGRFFGKSRKQYLKSDDFLNSTDPTYNFQKLHQFAAEQRVKLGLEK SDTDTLVAILKNNPEECRAYIESKKPGLGNFSEGNVHGWLKEEYTPTIPPKAINKSTGVL SDEAIKRIKEQARDLLLL
Mechanism of inhibition of retromer transport by the bacterial effector RidL. Yao, J., Yang, F., Sun, X. et al. Proc Natl Acad Sci U S A (2018) 115:E1446-E1454. DOI 10.1073/pnas.1717383115 · 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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