› 2lcr

Solution NMR

NMR Structure of Alk1 extracellular domain

Released:
DOI: 10.2210/pdb2lcr/pdb
PDB entry 2lcr coloured by chain, ensemble of 15 models, front view.
PDB entry 2lcr coloured by chain, ensemble of 15 models, side view.
PDB entry 2lcr coloured by chain, ensemble of 15 models, top view.
Source organism: Homo sapiens
Primary publication:
Structure of the Alk1 extracellular domain and characterization of its bone morphogenetic protein (BMP) binding properties.
Mahlawat P, Ilangovan U, Biswas T, Sun LZ, Hinck AP
Biochemistry 51 6328-41 (2012)
PMID: 22799562

Function and Biology Details

Reaction catalysed: 
ATP + [receptor-protein] = ADP + [receptor-protein] phosphate
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-153326 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serine/threonine-protein kinase receptor R3 Chain: A
Molecule details ›
Chain: A
Length: 101 amino acids
Theoretical weight: 11.15 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P37023 (Residues: 22-118; Coverage: 20%)
Gene names: ACVRL1, ACVRLK1, ALK1
Structure domains: CD59

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 80%
Refinement method: simulated annealing
Expression system: Escherichia coli

Quick links

Citations

11 review citations

Structural Biology and Evolution of the TGF-β Family.
Hinck et al. (2016)
10 more

1 mention without citation

Structure of the Alk1 extracellular domain and characterization of its bone morphogenetic protein (BMP) binding properties.
Mahlawat et al. (2012)