Crystal structure of human Vps29 complexed with RaPID-derived cyclic peptide RT-L1. Determined by X-ray diffraction at 2.69 Å resolution. Released 21 Jul 2021.
Explore 6XS9 in 3D Show helices and sheets RCSB PDB PDBe
6XS9 contains 8 α-helices and 37 β-strands across 6 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 |
| β-strand | 90 | 1 | 4 |
| α-helix | 96-106 | 11 | |
| β-strand | 110-112 | 3 | 3 |
| β-strand | 120-124 | 5 | 3 |
| β-strand | 127-131 | 5 | 3 |
| α-helix | 146-148 | 3 | |
| β-strand | 149-156 | 8 | 1 |
| β-strand | 159-168 | 10 | 1 |
| β-strand | 171-180 | 10 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 1-6 | 6 | 5 |
| α-helix | 20-25 | 6 | |
| β-strand | 33-36 | 4 | 5 |
| α-helix | 44-52 | 9 | |
| β-strand | 55-58 | 4 | 5 |
| β-strand | 72-77 | 6 | 6 |
| β-strand | 80-85 | 6 | 6 |
| α-helix | 96-106 | 11 | |
| β-strand | 110-113 | 4 | 6 |
| β-strand | 119-124 | 6 | 6 |
| β-strand | 127-132 | 6 | 6 |
| β-strand | 134 | 1 | 7 |
| α-helix | 146-147 | 2 | |
| β-strand | 148 | 1 | 7 |
| β-strand | 149-156 | 8 | 5 |
| β-strand | 159-168 | 10 | 5 |
| β-strand | 171-180 | 10 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2 | 1 | 8 |
| β-strand | 9 | 1 | 8 |
| β-strand | 11 | 1 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-4 | 3 | 10 |
| β-strand | 7-9 | 3 | 10 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Vacuolar protein sorting-associated protein 29 | A | protein | 192 | Homo sapiens | Q9UBQ0 (AlphaFold model) |
| Vacuolar protein sorting-associated protein 29 | B | protein | 192 | Homo sapiens | Q9UBQ0 (AlphaFold model) |
| 48V-tyr-ile-lys-thr-pro-leu-gly-thr-phe-pro-asn-arg-his-gly | C, D, E, F | protein | 15 | synthetic construct |
>6XS9_1 Vacuolar protein sorting-associated protein 29 (chains A) GSPEFGTRDRMLVLVLGDLHIPHRCNSLPAKFKKLLVPGKIQHILCTGNLCTKESYDYLK TLAGDVHIVRGDFDENLNYPEQKVVTVGQFKIGLIHGHQVIPWGDMASLALLQRQFDVDI LISGHTHKFEAFEHENKFYINPGSATGAYNALETNIIPSFVLMDIQASTVVTYVYQLIGD DVKVERIEYKKP
>6XS9_2 Vacuolar protein sorting-associated protein 29 (chains B) GSPEFGTRDRMLVLVLGDLHIPHRCNSLPAKFKKLLVPGKIQHILCTGNLCTKESYDYLK TLAGDVHIVRGDFDENLNYPEQKVVTVGQFKIGLIHGHQVIPWGDMASLALLQRQFDVDI LISGHTHKFEAFEHENKFYINPGSATGAYNALETNIIPSFVLMDIQASTVVTYVYQLIGD DVKVERIEYKKP
>6XS9_3 48V-TYR-ILE-LYS-THR-PRO-LEU-GLY-THR-PHE-PRO-ASN-ARG-HIS-GLY (chains C, D, E, F) XYIKTPLGTFPNRHG
Water and common crystallization additives (GOL) are not listed.
De novo macrocyclic peptides for inhibiting, stabilizing, and probing the function of the retromer endosomal trafficking complex. Chen, K.E., Guo, Q., Hill, T.A. et al. Sci Adv (2021) 7:eabg4007-eabg4007. DOI 10.1126/sciadv.abg4007 · 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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