› 2nca

Solution NMR

Structural Model for the N-terminal Domain of Human Cdc37

Released:
DOI: 10.2210/pdb2nca/pdb
PDB entry 2nca coloured by chain, ensemble of 20 models, front view.
PDB entry 2nca coloured by chain, ensemble of 20 models, side view.
PDB entry 2nca coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
Molecular Mechanism of Protein Kinase Recognition and Sorting by the Hsp90 Kinome-Specific Cochaperone Cdc37.
Keramisanou D, Aboalroub A, Zhang Z, Liu W, Marshall D, Diviney A, Larsen RW, Landgraf R, Gelis I
Mol Cell 62 260-271 (2016)
PMID: 27105117

Function and Biology Details

Biochemical function:
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: 128 amino acids
Theoretical weight: 15.41 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q16543 (Residues: 1-126; Coverage: 33%)
Gene names: CDC37, CDC37A
Sequence domains: Cdc37 N terminal kinase binding

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 25%
Refinement method: simulated annealing
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

9 review citations

The HSP90 chaperone machinery.
Schopf et al. (2017)
8 more

3 mentions without citation

Molecular Mechanism of Protein Kinase Recognition and Sorting by the Hsp90 Kinome-Specific Cochaperone Cdc37.
Keramisanou et al. (2016)
2 more