Solution structure of the full length sorting nexin 3. Determined by solution NMR. Released 4 May 2016.
Explore 2MXC in 3D Show helices and sheets RCSB PDB PDBe
2MXC contains 5 α-helices and 3 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 | 29-38 | 10 | 1 |
| β-strand | 47-55 | 9 | 1 |
| β-strand | 64-70 | 7 | 1 |
| α-helix | 71-84 | 14 | |
| α-helix | 89-92 | 4 | |
| α-helix | 97-99 | 3 | |
| α-helix | 112-129 | 18 | |
| α-helix | 140-145 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Sorting nexin-3 | A | protein | 172 | Homo sapiens | O60493 (AlphaFold model) |
>2MXC_1 Sorting nexin-3 (chains A) MAHHHHHHVGTAETVADTRRLITKPQNLNDAYGPPSNFLEIDVSNPQTVGVGRGRFTTYE IRVKTNLPIFKLKESTVRRRYSDFEWLRSELERESKVVVPPLPGKAFLRQLPFRGDDGIF DDNFIEERKQGLEQFINKVAGHPLAQNERCLHMFLQDEIIDKSYTPSKIRHA
Phosphorylation of conserved phosphoinositide binding pocket regulates sorting nexin membrane targeting. Lenoir, M., Ustunel, C., Rajesh, S. et al. Nat Commun (2018) 9:993-993. DOI 10.1038/s41467-018-03370-1 · PubMed
Other PDB entries of the same protein (UniProt O60493 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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