Function and Biology Details
Reactions catalysed:
Peptidylproline (omega=180) = peptidylproline (omega=0)
ATP + a protein = ADP + a phosphoprotein
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-154618 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Peptidyl-prolyl cis-trans isomerase FKBP1A
Molecule details ›
Chain: A
Length: 107 amino acids
Theoretical weight: 11.84 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: FKBP-type peptidyl-prolyl cis-trans isomerase
Structure domains: Chitinase A; domain 3
Length: 107 amino acids
Theoretical weight: 11.84 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
P62942 (Residues: 2-108; Coverage: 99%)
Sequence domains: FKBP-type peptidyl-prolyl cis-trans isomerase
Structure domains: Chitinase A; domain 3
Serine/threonine-protein kinase mTOR
Molecule details ›
Chain: B
Length: 94 amino acids
Theoretical weight: 11.33 KDa
Source organism: Homo sapiens
UniProt:
Sequence domains: FKBP12-rapamycin binding domain
Structure domains: FKBP12-rapamycin binding domain
Length: 94 amino acids
Theoretical weight: 11.33 KDa
Source organism: Homo sapiens
UniProt:
- Canonical: P42345 (Residues: 2019-2112; Coverage: 4%)
Sequence domains: FKBP12-rapamycin binding domain
Structure domains: FKBP12-rapamycin binding domain
