› 4bgg

X-ray diffraction
2.56Å resolution

Crystal structure of the ACVR1 kinase in complex with LDN-213844

Released:
DOI: 10.2210/pdb4bgg/pdb
PDB entry 4bgg coloured by chain, front view.
PDB entry 4bgg coloured by chain, side view.
PDB entry 4bgg coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure-activity relationship of 3,5-diaryl-2-aminopyridine ALK2 inhibitors reveals unaltered binding affinity for fibrodysplasia ossificans progressiva causing mutants.
Mohedas AH, Wang Y, Sanvitale CE, Canning P, Choi S, Xing X, Bullock AN, Cuny GD, Yu PB
J Med Chem 57 7900-15 (2014)
PMID: 25101911

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:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-170070 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Activin receptor type-1 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
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 844 4 x 844
Ligand FLC 7 x FLC
Ligand EDO 1 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04-1
Unit cell:
a: 85.38Å b: 99.85Å c: 187.438Å
α: 90° β: 92.93° γ: 90°
R-values:
R R work R free
0.217 0.215 0.247
Expression system: Spodoptera frugiperda

Quick links

Citations

21 review citations

Targeting BMP signalling in cardiovascular disease and anaemia.
Morrell et al. (2016)
20 more

5 mentions without citation

Recent Advances in ALK2 Inhibitors.
Rooney et al. (2021)
4 more