› 2qcq

X-ray diffraction
2.21Å resolution

Crystal structure of Bone Morphogenetic Protein-3 (BMP-3)

Released:
DOI: 10.2210/pdb2qcq/pdb
PDB entry 2qcq coloured by chain, front view.
PDB entry 2qcq coloured by chain, side view.
PDB entry 2qcq coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
BMP-3 and BMP-6 structures illuminate the nature of binding specificity with receptors.
Allendorph GP, Isaacs MJ, Kawakami Y, Izpisua Belmonte JC, Choe S
Biochemistry 46 12238-47 (2007)
PMID: 17924656

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-146290 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bone morphogenetic protein 3 Chains: A, B
Molecule details ›
Chains: A, B
Length: 110 amino acids
Theoretical weight: 12.42 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P12645 (Residues: 363-472; Coverage: 24%)
Gene names: BMP3, BMP3A
Sequence domains: Transforming growth factor beta like domain
Structure domains: Cystine-knot cytokines

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.3.1
Spacegroup: R3
Unit cell:
a: 96.85Å b: 96.85Å c: 101.48Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.23 0.228 0.257
Expression system: Escherichia coli BL21

Quick links

Citations

24 review citations

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

2 mentions without citation

The dipeptidyl peptidase IV inhibitors vildagliptin and K-579 inhibit a phospholipase C: a case of promiscuous scaffolds in proteins.
Chakraborty et al. (2013)
1 more