Function and Biology Details
Biochemical function:
Biological process:
Cellular component:
- not assigned
Sequence domains:
Structure domains:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-136257 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
ATP-dependent molecular chaperone HSP82
Molecule details ›
Chain: A
Length: 214 amino acids
Theoretical weight: 24.21 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
Sequence domains: Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase
Structure domains: Histidine kinase-like ATPase, C-terminal domain
Length: 214 amino acids
Theoretical weight: 24.21 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
- Canonical:
P02829 (Residues: 1-214; Coverage: 30%)
Sequence domains: Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase
Structure domains: Histidine kinase-like ATPase, C-terminal domain
Hsp90 co-chaperone Cdc37, N-terminally processed
Molecule details ›
Chain: B
Length: 265 amino acids
Theoretical weight: 30.87 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains:
Structure domains:
Length: 265 amino acids
Theoretical weight: 30.87 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical: Q16543 (Residues: 127-378; Coverage: 67%)
Sequence domains:
Structure domains:
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
ESRF BEAMLINE ID14-4
Spacegroup:
P3121
Expression system: Escherichia coli
