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X-ray diffraction
2Å resolution

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

Released:
DOI: 10.2210/pdb3oom/pdb
PDB entry 3oom coloured by chain, front view.
PDB entry 3oom coloured by chain, side view.
PDB entry 3oom coloured by chain, top view.
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:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-170071 (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 tyrosine and serine/threonine kinase
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand PO4 2 x PO4
Ligand 507 1 x 507
Ligand EDO 15 x EDO
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

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