Function and Biology Details
Reactions catalysed:
Peptidylproline (omega=180) = peptidylproline (omega=0)
ATP + a protein = ADP + a phosphoprotein
Biochemical function:
Biological process:
- not assigned
Cellular component:
- not assigned
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-154622 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Peptidyl-prolyl cis-trans isomerase FKBP5
Molecule details ›
Chains: A, D
Length: 144 amino acids
Theoretical weight: 15.69 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: FKBP-type peptidyl-prolyl cis-trans isomerase
Structure domains: Chitinase A; domain 3
Length: 144 amino acids
Theoretical weight: 15.69 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
Q13451 (Residues: 1-140; Coverage: 31%)
Sequence domains: FKBP-type peptidyl-prolyl cis-trans isomerase
Structure domains: Chitinase A; domain 3
Serine/threonine-protein kinase mTOR
Molecule details ›
Chains: B, E
Length: 98 amino acids
Theoretical weight: 11.75 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: FKBP12-rapamycin binding domain
Structure domains: FKBP12-rapamycin binding domain
Length: 98 amino acids
Theoretical weight: 11.75 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical: P42345 (Residues: 2025-2114; Coverage: 4%)
Sequence domains: FKBP12-rapamycin binding domain
Structure domains: FKBP12-rapamycin binding domain
