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RADICICOL BOUND TO THE ATP BINDING SITE OF THE N-TERMINAL DOMAIN OF THE YEAST HSP90 CHAPERONE

X-ray diffraction
2.5Å resolution
PDB entry 1bgq coloured by chain, front view.
PDB entry 1bgq coloured by chain, side view.
PDB entry 1bgq coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Assembly composition:
homo dimer (preferred)
Entry contents: 1 distinct polypeptide molecule

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Assemblies

Assembly 1 (preferred)
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Assembly Name: ATP-dependent molecular chaperone HSP82
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Multimeric state: homo dimer
Accessible surface area: 18934.77 Å2
Buried surface area: 3562.15 Å2
Dissociation area: 1,105.8 Å2
Dissociation energy (ΔGdiss): 1.58 kcal/mol
Dissociation entropy (TΔSdiss): 12.81 kcal/mol
Symmetry number: 2
PDBe Complex ID: PDB-CPX-136258

Macromolecules

ATP-dependent molecular chaperone HSP82
Chain: A
Length: 225 amino acids
Theoretical weight: 25.53 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
  • Canonical: P02829 (Residues: 1-214; Coverage: 30%)
Gene names: HSP82, HSP90, YPL240C
Pfam: Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase
InterPro:
CATH: Histidine kinase-like ATPase, C-terminal domain
SCOP: Heat shock protein 90, HSP90, N-terminal domain
ATP-dependent molecular chaperone HSP82 in PDB entry 1bgq, assembly 1, front view.
ATP-dependent molecular chaperone HSP82 in PDB entry 1bgq, assembly 1, side view.
ATP-dependent molecular chaperone HSP82 in PDB entry 1bgq, assembly 1, top view.
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