PDBe 3h9r

X-ray diffraction
2.35Å resolution

Crystal structure of the kinase domain of type I activin receptor (ACVR1) in complex with FKBP12 and dorsomorphin


Function and Biology Details

Reactions catalysed:
ATP + [receptor-protein] = ADP + [receptor-protein] phosphate. 
Peptidylproline (omega=180) = peptidylproline (omega=0). 
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Activin receptor type-1 Chain: A
Molecule details ›
Chain: A
Length: 330 amino acids
Theoretical weight: 37.4 KDa
Source organism: Homo sapiens
Expression system: unidentified baculovirus
  • Canonical: Q04771 (Residues: 172-499; Coverage: 67%)
Gene names: ACVR1, ACVRLK2
Sequence domains:
Structure domains:
Peptidyl-prolyl cis-trans isomerase FKBP1A Chain: B
Molecule details ›
Chain: B
Length: 109 amino acids
Theoretical weight: 12.05 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
  • Canonical: P62942 (Residues: 1-108; Coverage: 100%)
Gene names: FKBP1, FKBP12, FKBP1A
Sequence domains: FKBP-type peptidyl-prolyl cis-trans isomerase

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I02
Spacegroup: P212121
Unit cell:
a: 43.349Å b: 62.345Å c: 171.597Å
α: 90° β: 90° γ: 90°
R R work R free
0.187 0.187 0.256
Expression systems:
  • unidentified baculovirus
  • Escherichia coli