PDBe 3soc

X-ray diffraction
1.95Å resolution

Crystal structure of Activin receptor type-IIA (ACVR2A) kinase domain in complex with a quinazolin

Released:
Source organism: Homo sapiens
Entry authors: Chaikuad A, Williams E, Mahajan P, Cooper CDO, Sanvitale C, Vollmar M, Muniz JRC, Yue WW, 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:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Activin receptor type-2A Chains: A, B
Molecule details ›
Chains: A, B
Length: 322 amino acids
Theoretical weight: 36.55 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P27037 (Residues: 191-488; Coverage: 60%)
Gene names: ACVR2, ACVR2A
Sequence domains: Protein kinase domain
Structure domains:

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I02
Spacegroup: P6522
Unit cell:
a: 110.68Å b: 110.68Å c: 208.061Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.165 0.163 0.211
Expression system: Spodoptera frugiperda