PDBe 1rew

X-ray diffraction
1.86Å resolution

Structural refinement of the complex of bone morphogenetic protein 2 and its type IA receptor

Released:
Source organism: Homo sapiens
Primary publication:
Molecular recognition of BMP-2 and BMP receptor IA.
Nat. Struct. Mol. Biol. 11 481-8 (2004)
PMID: 15064755

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Bone morphogenetic protein 2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 114 amino acids
Theoretical weight: 12.92 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P12643 (Residues: 283-396; Coverage: 31%)
Gene names: BMP2, BMP2A
Sequence domains: Transforming growth factor beta like domain
Structure domains: Cystine-knot cytokines
Bone morphogenetic protein receptor type-1A Chains: C, D
Molecule details ›
Chains: C, D
Length: 135 amino acids
Theoretical weight: 14.67 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P36894 (Residues: 24-152; Coverage: 25%)
Gene names: ACVRLK3, ALK3, BMPR1A
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: SLS BEAMLINE X06SA
Spacegroup: P65
Unit cell:
a: 107.493Å b: 107.493Å c: 102.282Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.208 0.207 0.229
Expression system: Escherichia coli