HSP90 co-chaperone CDC37. Determined by X-ray diffraction at 1.88 Å resolution. Released 9 Dec 2008.
Explore 2W0G in 3D Show helices and sheets RCSB PDB PDBe
2W0G contains 7 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 | 149-163 | 15 | |
| α-helix | 168-177 | 10 | |
| α-helix | 179-181 | 3 | |
| α-helix | 184-199 | 16 | |
| α-helix | 203-226 | 24 | |
| α-helix | 230-241 | 12 | |
| α-helix | 247-272 | 26 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| HSP90 co-chaperone CDC37 | A | protein | 129 | HOMO SAPIENS | Q16543 (AlphaFold model) |
>2W0G_1 HSP90 CO-CHAPERONE CDC37 (chains A) HKTFVEKYEKQIKHFGMLRRWDDSQKYLSDNVHLVCEETANYLVIWCIDLEVEEKCALME QVAHQTIVMQFILELAKSLKVDPRACFRQFFTKIKTADRQYMEGFNDELEAFKERVRGRA KLRIEKAMK
The Human Cdc37.Hsp90 Complex Studied by Heteronuclear NMR Spectroscopy. Sreeramulu, S., Jonker, H.R.A., Richter, C. et al. J Biol Chem (2009) 284:3885. DOI 10.1074/JBC.M806715200 · PubMed
Other PDB entries of the same protein (UniProt Q16543 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 2W0G directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.