Function and Biology Details
Biochemical function:
Biological process:
Cellular component:
- not assigned
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-136255 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
ATP-dependent molecular chaperone HSP82
Molecule details ›
Chain: A
Length: 260 amino acids
Theoretical weight: 30.49 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
Sequence domains: Hsp90 protein
Structure domains:
Length: 260 amino acids
Theoretical weight: 30.49 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
- Canonical:
P02829 (Residues: 273-530; Coverage: 36%)
Sequence domains: Hsp90 protein
Structure domains:
Hsp90 co-chaperone AHA1
Molecule details ›
Chain: B
Length: 170 amino acids
Theoretical weight: 19.12 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
Sequence domains: Activator of Hsp90 ATPase, N-terminal
Structure domains: Activator of Hsp90 ATPase Aha1, N-terminal domain
Length: 170 amino acids
Theoretical weight: 19.12 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
- Canonical: Q12449 (Residues: 1-156; Coverage: 45%)
Sequence domains: Activator of Hsp90 ATPase, N-terminal
Structure domains: Activator of Hsp90 ATPase Aha1, N-terminal domain
