Function and Biology Details
Reactions catalysed:
ATP + [receptor-protein] = ADP + [receptor-protein] phosphate
Peptidylproline (omega=180) = peptidylproline (omega=0)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- GS domain
- FKBP-type peptidyl-prolyl cis-trans isomerase domain
- Protein kinase domain
- Peptidyl-prolyl cis-trans isomerase domain superfamily
- Serine/threonine-protein kinase, active site
- Protein kinase, ATP binding site
- Serine-threonine/tyrosine-protein kinase, catalytic domain
- Protein kinase-like domain superfamily
1 more domain
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-158813 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Activin receptor type-1
Molecule details ›
Chain: A
Length: 330 amino acids
Theoretical weight: 37.4 KDa
Source organism: Homo sapiens
Expression system: unidentified baculovirus
UniProt:
Sequence domains:
Structure domains:
Length: 330 amino acids
Theoretical weight: 37.4 KDa
Source organism: Homo sapiens
Expression system: unidentified baculovirus
UniProt:
- Canonical:
Q04771 (Residues: 172-499; Coverage: 67%)
Sequence domains:
Structure domains:
Peptidyl-prolyl cis-trans isomerase FKBP1A
Molecule details ›
Chain: B
Length: 109 amino acids
Theoretical weight: 12.05 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: 109 amino acids
Theoretical weight: 12.05 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical: P62942 (Residues: 1-108; Coverage: 100%)
Sequence domains: FKBP-type peptidyl-prolyl cis-trans isomerase
Structure domains: Chitinase A; domain 3
