PDBe 3oom

X-ray diffraction
2Å resolution

Crystal structure of the ACVR1 kinase domain in complex with the imidazo[1,2-b]pyridazine inhibitor K00507

Released:
Source organism: Homo sapiens
Entry authors: Chaikuad A, Sanvitale C, Cooper C, Mahajan P, Daga N, Petrie K, Alfano I, Gileadi O, Fedorov O, Allerston C, Krojer T, von Delft F, Weigelt J, Arrowsmith CH, Edwards AM, Bountra C, Bullock A, Structural Genomics Consortium (SGC)

Function and Biology Details

Reaction catalysed:
ATP + [receptor-protein] = ADP + [receptor-protein] phosphate. 
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Activin receptor type-1 Chain: A
Molecule details ›
Chain: A
Length: 301 amino acids
Theoretical weight: 34.54 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: Q04771 (Residues: 201-499; Coverage: 61%)
Gene names: ACVR1, ACVRLK2
Sequence domains: Protein kinase domain
Structure domains:

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I03
Spacegroup: C2221
Unit cell:
a: 58.4Å b: 88.03Å c: 138.97Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.169 0.166 0.231
Expression system: Spodoptera frugiperda