› 2bhk

X-ray diffraction
2.4Å resolution

Crystal structure of human growth and differentiation factor 5 (GDF5)

Released:
DOI: 10.2210/pdb2bhk/pdb
PDB entry 2bhk coloured by chain, front view.
PDB entry 2bhk coloured by chain, side view.
PDB entry 2bhk coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure of recombinant human growth and differentiation factor 5: evidence for interaction of the type I and type II receptor-binding sites.
Schreuder H, Liesum A, Pohl J, Kruse M, Koyama M
Biochem Biophys Res Commun 329 1076-86 (2005)
PMID: 15752764

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-154934 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Growth/differentiation factor 5 Chain: A
Molecule details ›
Chain: A
Length: 120 amino acids
Theoretical weight: 13.6 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P43026 (Residues: 382-501; Coverage: 25%)
Gene names: BMP14, CDMP1, GDF5
Sequence domains: Transforming growth factor beta like domain
Structure domains: Cystine-knot cytokines

Ligands and Environments

1 bound ligand:
Ligand IPA 5 x IPA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ENRAF-NONIUS FR571
Spacegroup: P3221
Unit cell:
a: 98.2Å b: 98.2Å c: 43.7Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.168 0.168 0.22
Expression system: Escherichia coli

Quick links

Citations

14 review citations

Bone Morphogenetic Proteins.
Katagiri et al. (2016)
13 more

4 mentions without citation

Mechanical strength of 17,134 model proteins and cysteine slipknots.
Sikora et al. (2009)
3 more