Structural Model for the N-terminal Domain of Human Cdc37. Determined by solution NMR. Released 4 May 2016.
Explore 2NCA in 3D Show helices and sheets RCSB PDB PDBe
2NCA contains 3 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 | 26-72 | 47 | |
| α-helix | 79-109 | 31 | |
| α-helix | 113-116 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Hsp90 co-chaperone Cdc37 | A | protein | 128 | Homo sapiens | Q16543 (AlphaFold model) |
>2NCA_1 Hsp90 co-chaperone Cdc37 (chains A) GHMVDYSVWDHIEVSDDEDETHPNIDTASLFRWRHQARVERMEQFQKEKEELDRGCRECK RKVAECQRKLKELEVAEGGKAELERLQAEAQQLRKEERSWEQKLEEMRKKEKSMPWNVDT LSKDGFSK
Molecular Mechanism of Protein Kinase Recognition and Sorting by the Hsp90 Kinome-Specific Cochaperone Cdc37. Keramisanou, D., Aboalroub, A., Zhang, Z. et al. Mol Cell (2016) 62:260-271. DOI 10.1016/j.molcel.2016.04.005 · 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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