2NCA: Hsp90 co-chaperone Cdc37

Structural Model for the N-terminal Domain of Human Cdc37. Determined by solution NMR. Released 4 May 2016.

Method
Solution NMR
Organism
Homo sapiens
Chains
1
Atoms
1,062
Mol. weight
15.41 kDa
Released
4 May 2016

Explore 2NCA in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 3 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix26-7247
α-helix79-10931
α-helix113-1164

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Hsp90 co-chaperone Cdc37Aprotein128Homo sapiensQ16543 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2NCA_1 Hsp90 co-chaperone Cdc37 (chains A)
GHMVDYSVWDHIEVSDDEDETHPNIDTASLFRWRHQARVERMEQFQKEKEELDRGCRECK
RKVAECQRKLKELEVAEGGKAELERLQAEAQQLRKEERSWEQKLEEMRKKEKSMPWNVDT
LSKDGFSK

Primary citation

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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