› 2n5x

Solution NMR

C-terminal domain of Cdc37 cochaperone

Released:
DOI: 10.2210/pdb2n5x/pdb
PDB entry 2n5x coloured by chain, ensemble of 10 models, front view.
PDB entry 2n5x coloured by chain, ensemble of 10 models, side view.
PDB entry 2n5x coloured by chain, ensemble of 10 models, top view.
Source organism: Homo sapiens
Primary publication:
The C-terminal domain of human Cdc37 studied by solution NMR.
Zhang Z, Keramisanou D, Dudhat A, Paré M, Gelis I
J Biomol NMR 63 315-21 (2015)
PMID: 26400850

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-172489 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Hsp90 co-chaperone Cdc37, N-terminally processed Chain: A
Molecule details ›
Chain: A
Length: 94 amino acids
Theoretical weight: 10.2 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q16543 (Residues: 288-378; Coverage: 24%)
Gene names: CDC37, CDC37A
Sequence domains: Cdc37 C terminal domain
Structure domains: Helix Hairpins

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 90%
Refinement method: simulated annealing
Expression system: Escherichia coli

Quick links

Citations

1 review citation

A guide to quantifying membrane protein dynamics in lipids and other native-like environments by solution-state NMR spectroscopy.
Bibow et al. (2019)
2 other articles

4 mentions without citation

How Hsp90 and Cdc37 Lubricate Kinase Molecular Switches.
Verba et al. (2017)
3 more