Crystal structure of mouse VPS29 complexed with Mn2+. Determined by X-ray diffraction at 2.4 Å resolution. Released 15 Dec 2010.
Explore 3PSN in 3D Show helices and sheets RCSB PDB PDBe
3PSN contains 6 α-helices and 24 β-strands across 2 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 |
| α-helix | 20-23 | 4 | |
| 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 | 80-85 | 6 | 2 |
| β-strand | 91 | 1 | 3 |
| α-helix | 96-106 | 11 | |
| β-strand | 110-113 | 4 | 2 |
| β-strand | 120-124 | 5 | 2 |
| β-strand | 127-131 | 5 | 2 |
| β-strand | 149-156 | 8 | 1 |
| β-strand | 159-168 | 10 | 1 |
| β-strand | 171-180 | 10 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-6 | 5 | 4 |
| α-helix | 20-23 | 4 | |
| β-strand | 33-36 | 4 | 4 |
| α-helix | 43-52 | 10 | |
| β-strand | 55-58 | 4 | 4 |
| β-strand | 72-77 | 6 | 5 |
| β-strand | 80-85 | 6 | 5 |
| β-strand | 91 | 1 | 3 |
| α-helix | 96-106 | 11 | |
| β-strand | 110-113 | 4 | 5 |
| β-strand | 120-124 | 5 | 5 |
| β-strand | 127-131 | 5 | 5 |
| β-strand | 149-156 | 8 | 4 |
| β-strand | 159-168 | 10 | 4 |
| β-strand | 171-180 | 10 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Vacuolar protein sorting-associated protein 29 | A, B | protein | 192 | Mus musculus | Q9QZ88 (AlphaFold model) |
>3PSN_1 Vacuolar protein sorting-associated protein 29 (chains A, B) GSPEFGTRDRMLVLVLGDLHIPHRCNSLPAKFKKLLVPGKIQHILCTGNLCTKESYDYLK TLAGDVHIVRGDFDENLNYPEQKVVTVGQFKIGLIHGHQVIPWGDMASLALLQRQFDVDI LISGHTHKFEAFEHENKFYINPGSATGAYNALETNIIPSFVLMDIQASTVVTYVYQLIGD DVKVERIEYKKS
| ID | Name | Formula | Copies |
|---|---|---|---|
| MN | Manganese (II) ion | Mn | 6 |
Conformational dynamics and biomolecular interactions of VPS29 studied by NMR and X-ray crystallography. Swarbrick, J., Shaw, D., Chhabra, S. et al. To be published.
Other PDB entries of the same protein (UniProt Q9QZ88 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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