Function and Biology Details
Reaction catalysed:
ATP + H(2)O = ADP + phosphate
Biochemical function:
Biological process:
Cellular component:
- not assigned
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139821 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Heat shock protein HSP 90-alpha
Molecule details ›
Chain: A
Length: 210 amino acids
Theoretical weight: 23.54 KDa
Source organism: Homo sapiens
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: 210 amino acids
Theoretical weight: 23.54 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
P07900 (Residues: 14-223; Coverage: 29%)
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: 129 amino acids
Theoretical weight: 15.52 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: Cdc37 Hsp90 binding domain
Structure domains: Cdc37, Hsp90 binding domain
Length: 129 amino acids
Theoretical weight: 15.52 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical: Q16543 (Residues: 148-276; Coverage: 34%)
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
Refinement method:
simulated annealing, torsion angle dynamics
Expression system: Escherichia coli
