› 2w0g

X-ray diffraction
1.88Å resolution

HSP90 CO-CHAPERONE CDC37

Released:
DOI: 10.2210/pdb2w0g/pdb
PDB entry 2w0g coloured by chain, front view.
PDB entry 2w0g coloured by chain, side view.
PDB entry 2w0g coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The human Cdc37.Hsp90 complex studied by heteronuclear NMR spectroscopy.
Sreeramulu S, Jonker HR, Langer T, Richter C, Lancaster CR, Schwalbe H
J Biol Chem 284 3885-96 (2009)
PMID: 19073599

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: 129 amino acids
Theoretical weight: 15.52 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q16543 (Residues: 148-276; Coverage: 34%)
Gene names: CDC37, CDC37A
Sequence domains: Cdc37 Hsp90 binding domain
Structure domains: Cdc37, Hsp90 binding domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007
Spacegroup: P61
Unit cell:
a: 48.67Å b: 48.67Å c: 104.257Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.213 0.212 0.246
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

6 review citations

Recent advances in the development of protein-protein interactions modulators: mechanisms and clinical trials.
Lu et al. (2020)
5 more

4 mentions without citation

Protein-protein docking benchmark version 4.0.
Hwang et al. (2010)
3 more