C-terminal domain of Cdc37 cochaperone. Determined by solution NMR. Released 7 Oct 2015.
Explore 2N5X in 3D Show helices and sheets RCSB PDB PDBe
2N5X contains 4 α-helices and 0 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 |
|---|---|---|---|
| α-helix | 294-299 | 6 | |
| α-helix | 303-310 | 8 | |
| α-helix | 314-323 | 10 | |
| α-helix | 326-338 | 13 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Hsp90 co-chaperone Cdc37 | A | protein | 94 | Homo sapiens | Q16543 (AlphaFold model) |
>2N5X_1 Hsp90 co-chaperone Cdc37 (chains A) GHMGPGGLDPVEVYESLPEELQKCFDVKDVQMLQDAISKMDPTDAKYHMQRCIDSGLWVP NSKASEAKEGEEAGPGDPLLEAVPKTGDEKDVSV
The C-terminal domain of human Cdc37 studied by solution NMR. Zhang, Z., Keramisanou, D., Dudhat, A. et al. J Biomol NMR (2015) 63:315-321. DOI 10.1007/s10858-015-9988-6 · PubMed
Other PDB entries of the same protein (UniProt Q16543 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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