Function and Biology Details
Reactions catalysed:
[a protein]-serine/threonine phosphate + H(2)O = [a protein]-serine/threonine + phosphate
ATP + H(2)O = ADP + phosphate
Biochemical function:
- not assigned
Biological process:
- not assigned
Cellular component:
- not assigned
Sequence domains:
Structure domain:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139820 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Serine/threonine-protein phosphatase 5
Molecule details ›
Chain: A
Length: 140 amino acids
Theoretical weight: 16.21 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: Tetratricopeptide repeat
Structure domains: Tetratricopeptide repeat domain
Length: 140 amino acids
Theoretical weight: 16.21 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
P53041 (Residues: 18-147; Coverage: 26%)
Sequence domains: Tetratricopeptide repeat
Structure domains: Tetratricopeptide repeat domain
Heat shock protein HSP 90-alpha
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
Chemical shift assignment:
87%
Refinement method:
ARIA
Expression systems:
- Escherichia coli BL21(DE3)
- Not provided
