› 1waq

X-ray diffraction
2.28Å resolution

Crystal structure of human Growth and Differentiation Factor 5 (GDF-5)

Released:
DOI: 10.2210/pdb1waq/pdb
PDB entry 1waq coloured by chain, front view.
PDB entry 1waq coloured by chain, side view.
PDB entry 1waq coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
A single residue of GDF-5 defines binding specificity to BMP receptor IB.
Nickel J, Kotzsch A, Sebald W, Mueller TD
J Mol Biol 349 933-47 (2005)
PMID: 15890363

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: 117 amino acids
Theoretical weight: 13.41 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P43026 (Residues: 387-501; Coverage: 24%)
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 MPD 3 x MPD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P3221
Unit cell:
a: 97.771Å b: 97.771Å c: 43.325Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.223 0.222 0.237
Expression system: Escherichia coli

Quick links

Citations

23 review citations

Cellular and molecular basis of pulmonary arterial hypertension.
Morrell et al. (2009)
22 more

12 mentions without citation

Structure-guided engineering of TGF-βs for the development of novel inhibitors and probing mechanism.
Hinck AP. (2018)
11 more