› 3bmp

X-ray diffraction
2.7Å resolution

HUMAN BONE MORPHOGENETIC PROTEIN-2 (BMP-2)

Released:
DOI: 10.2210/pdb3bmp/pdb
PDB entry 3bmp coloured by chain, front view.
PDB entry 3bmp coloured by chain, side view.
PDB entry 3bmp coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure of human bone morphogenetic protein-2 at 2.7 A resolution.
Scheufler C, Sebald W, Hülsmeyer M
J Mol Biol 287 103-15 (1999)
PMID: 10074410

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-146279 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bone morphogenetic protein 2 Chain: A
Molecule details ›
Chain: A
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

Ligands and Environments

1 bound ligand:
Ligand MPD 1 x MPD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: R32
Unit cell:
a: 91.44Å b: 91.44Å c: 107.75Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.242 0.242 0.278
Expression system: Escherichia coli

Quick links

Citations

37 review citations

Growth factor delivery-based tissue engineering: general approaches and a review of recent developments.
Lee et al. (2011)
36 more

24 mentions without citation

TGF-β/BMP signaling and other molecular events: regulation of osteoblastogenesis and bone formation.
Rahman et al. (2015)
23 more