Crystal structure of human vps26. Determined by X-ray diffraction at 2.1 Å resolution. Released 30 May 2006.
Explore 2FAU in 3D Show helices and sheets RCSB PDB PDBe
2FAU contains 5 α-helices and 27 β-strands across 1 chain. 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 | 12-18 | 7 | 1 |
| α-helix | 21-23 | 3 | |
| β-strand | 26-30 | 5 | 2 |
| β-strand | 36-40 | 5 | 2 |
| β-strand | 41-42 | 2 | 3 |
| β-strand | 48-56 | 9 | 1 |
| β-strand | 63-65 | 3 | 4 |
| β-strand | 68-78 | 11 | 5 |
| β-strand | 85-96 | 12 | 5 |
| β-strand | 99-101 | 3 | 4 |
| β-strand | 105-111 | 7 | 1 |
| β-strand | 121-122 | 2 | 5 |
| β-strand | 126-136 | 11 | 5 |
| α-helix | 142 | 1 | |
| β-strand | 143-149 | 7 | 5 |
| β-strand | 150-151 | 2 | 3 |
| β-strand | 155 | 1 | 6 |
| β-strand | 164-170 | 7 | 7 |
| β-strand | 174-180 | 7 | 7 |
| β-strand | 184-186 | 3 | 8 |
| β-strand | 190-200 | 11 | 7 |
| β-strand | 204-217 | 14 | 9 |
| α-helix | 220-222 | 3 | |
| β-strand | 224-234 | 11 | 9 |
| β-strand | 246-251 | 6 | 7 |
| β-strand | 261-265 | 5 | 9 |
| β-strand | 268-280 | 13 | 9 |
| β-strand | 285-292 | 8 | 9 |
| β-strand | 293-295 | 3 | 8 |
| α-helix | 296 | 1 | |
| β-strand | 297 | 1 | 6 |
| α-helix | 298 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Vacuolar protein sorting 26 | A | protein | 341 | Homo sapiens | O75436 (AlphaFold model) |
>2FAU_1 Vacuolar protein sorting 26 (chains A) MGMSFLGGFFGPICEIDIVLNDGETRKMAEMKTEDGKVEKHYLFYDGESVSGKVNLAFKQ PGKRLEHQGIRIEFVGQIELFNDKSNTHEFVNLVKELALPGELTQSRSYDFEFMQVEKPY ESYIGANVRLRYFLKVTIVRRLTDLVKEYDLIVHQLATYPDVNNSIKMEVGIEDCLHIEF EYNKSKYHLKDVIVGKIYFLLVRIKIQHMELQLIKKEITGIGPSTTTETETIAKYEIMDG APVKGESIPIRLFLAGYDPTPTMRDVNKKFSVRYFLNLVLVDEEDRRYFKQQEIILWRKA PEKLRKQRTNFHQRFESPESQASAEQPEMGLVPRGSHHHHH
The retromer subunit Vps26 has an arrestin fold and binds Vps35 through its C-terminal domain. Shi, H., Rojas, R., Bonifacino, J.S. et al. Nat Struct Mol Biol (2006) 13:540-548. DOI 10.1038/nsmb1103 · PubMed
Other PDB entries of the same protein (UniProt O75436 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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