› 2h64

X-ray diffraction
1.92Å resolution

Crystal structure of a ternary ligand-receptor complex of BMP-2

Released:
DOI: 10.2210/pdb2h64/pdb
PDB entry 2h64 coloured by chain, front view.
PDB entry 2h64 coloured by chain, side view.
PDB entry 2h64 coloured by chain, top view.
Source organisms:
Primary publication:
A silent H-bond can be mutationally activated for high-affinity interaction of BMP-2 and activin type IIB receptor.
Weber D, Kotzsch A, Nickel J, Harth S, Seher A, Mueller U, Sebald W, Mueller TD
OpenAccess logo BMC Struct Biol 7 6 (2007)
PMID: 17295905

Function and Biology Details

Reaction catalysed: 
ATP + [receptor-protein] = ADP + [receptor-protein] phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
hetero hexamer (preferred)
PDBe Complex ID:
PDB-CPX-536962 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Bone morphogenetic protein 2 Chain: A
Molecule details ›
Chain: A
Length: 114 amino acids
Theoretical weight: 12.94 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 Chain: B
Molecule details ›
Chain: B
Length: 129 amino acids
Theoretical weight: 14.2 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
Activin receptor type-2B Chain: C
Molecule details ›
Chain: C
Length: 99 amino acids
Theoretical weight: 11.65 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: P27040 (Residues: 19-117; Coverage: 19%)
Gene name: Acvr2b
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: RIGAKU
Spacegroup: P3221
Unit cell:
a: 82.79Å b: 82.79Å c: 111.12Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.232 0.228 0.264
Expression system: Escherichia coli

Quick links

Citations

17 review citations

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

15 mentions without citation

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