› 2hlq

X-ray diffraction
1.45Å resolution

Crystal Structure of the Extracellular Domain of the Type II BMP Receptor

Released:
DOI: 10.2210/pdb2hlq/pdb
PDB entry 2hlq coloured by chain, front view.
PDB entry 2hlq coloured by chain, side view.
PDB entry 2hlq coloured by chain, top view.
Source organism: Ovis aries
Primary publication:
High resolution structures of the bone morphogenetic protein type II receptor in two crystal forms: implications for ligand binding.
Mace PD, Cutfield JF, Cutfield SM
Biochem Biophys Res Commun 351 831-8 (2006)
PMID: 17094948

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 Chain: A
Molecule details ›
Chain: A
Length: 100 amino acids
Theoretical weight: 11.15 KDa
Source organism: Ovis aries
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q13873 (Residues: 33-131; Coverage: 10%)
Gene names: BMPR2, PPH1
Sequence domains: Activin types I and II receptor domain
Structure domains: CD59

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-1
Spacegroup: P212121
Unit cell:
a: 35.588Å b: 45.078Å c: 48.162Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.192 0.19 0.232
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

7 review citations

Promiscuity and specificity in BMP receptor activation.
Mueller et al. (2012)
6 more

11 mentions without citation

Pulmonary Arterial Hypertension: A Current Perspective on Established and Emerging Molecular Genetic Defects.
Machado et al. (2015)
10 more