› 3g2f

X-ray diffraction
2.35Å resolution

Crystal structure of the kinase domain of bone morphogenetic protein receptor type II (BMPR2) at 2.35 A resolution

Released:
DOI: 10.2210/pdb3g2f/pdb
PDB entry 3g2f coloured by chain, front view.
PDB entry 3g2f coloured by chain, side view.
PDB entry 3g2f coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural consequences of BMPR2 kinase domain mutations causing pulmonary arterial hypertension.
Chaikuad A, Thangaratnarajah C, von Delft F, Bullock AN
Sci Rep 9 18351 (2019)
PMID: 31797984

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-171828 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bone morphogenetic protein receptor type-2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 336 amino acids
Theoretical weight: 38.78 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q13873 (Residues: 189-517; Coverage: 33%)
Gene names: BMPR2, PPH1
Sequence domains: Protein kinase domain
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand ADP 2 x ADP
Ligand MG 2 x MG
Ligand SO4 2 x SO4
Ligand EDO 4 x EDO
1 modified residue:
Ligand CAS 6 x CAS

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P21212
Unit cell:
a: 94.54Å b: 218.793Å c: 44.187Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.21 0.208 0.246
Expression system: Escherichia coli

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Citations

4 citation in other articles

Fibroblast growth factors: the keepers of endothelial normalcy.
Simons M. (2021)
3 more

9 mentions without citation

Structural perspective of BMP ligands and signaling.
Gipson et al. (2020)
8 more