› 5i05

X-ray diffraction
1.87Å resolution

Crystal structure of human BMP9 at 1.87 A resolution

Released:
DOI: 10.2210/pdb5i05/pdb
PDB entry 5i05 coloured by chain, front view.
PDB entry 5i05 coloured by chain, side view.
PDB entry 5i05 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural Basis of the Human Endoglin-BMP9 Interaction: Insights into BMP Signaling and HHT1.
Saito T, Bokhove M, Croci R, Zamora-Caballero S, Han L, Letarte M, de Sanctis D, Jovine L
Cell Rep 19 1917-1928 (2017)
PMID: 28564608

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-193830 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Growth/differentiation factor 2 Chain: A
Molecule details ›
Chain: A
Length: 110 amino acids
Theoretical weight: 12.1 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
UniProt:
  • Canonical: Q9UK05 (Residues: 320-429; Coverage: 27%)
Gene names: BMP9, GDF2
Sequence domains: Transforming growth factor beta like domain

Ligands and Environments

1 bound ligand:
Ligand GOL 2 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I02
Spacegroup: I4122
Unit cell:
a: 71.06Å b: 71.06Å c: 145.67Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.216 0.214 0.233
Expression system: Homo sapiens

Quick links

Citations

26 review citations

Contextual determinants of TGFβ action in development, immunity and cancer.
David et al. (2018)
25 more

3 mentions without citation

Recombinant production, purification, crystallization, and structure analysis of human transforming growth factor β2 in a new conformation.
Del Amo-Maestro et al. (2019)
2 more