5uhm

X-ray diffraction
1.9Å resolution

Apo-Structure of Mature Growth Differentiation Factor 11

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Growth/differentiation factor 11 Chains: A, B
Molecule details ›
Chains: A, B
Length: 109 amino acids
Theoretical weight: 12.47 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O95390 (Residues: 299-407; Coverage: 29%)
Gene names: BMP11, GDF11
Sequence domains: Transforming growth factor beta like domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-D
Spacegroup: P3221
Unit cell:
a: 65.16Å b: 65.16Å c: 101.942Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.219 0.217 0.258
Expression system: Escherichia coli