PDBe 5mya

X-ray diffraction
2.9Å resolution

Homodimerization of Tie2 Fibronectin-like domains 1-3 in space group C2

Released:
Source organism: Homo sapiens
Primary publication:
Structural basis of Tie2 activation and Tie2/Tie1 heterodimerization.
Proc. Natl. Acad. Sci. U.S.A. (2017)
PMID: 28396439

Function and Biology Details

Reaction catalysed:
ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate
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:
Angiopoietin-1 receptor Chains: A, B
Molecule details ›
Chains: A, B
Length: 333 amino acids
Theoretical weight: 37.58 KDa
Source organism: Homo sapiens
Expression system: Spodoptera aff. frugiperda 2 RZ-2014
UniProt:
  • Canonical: Q02763 (Residues: 443-742; Coverage: 27%)
Gene names: TEK, TIE2, VMCM, VMCM1
Sequence domains: Fibronectin type III domain

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID30B
Spacegroup: C2
Unit cell:
a: 134.16Å b: 104.69Å c: 79.52Å
α: 90° β: 121.41° γ: 90°
R-values:
R R work R free
0.237 0.234 0.277
Expression system: Spodoptera aff. frugiperda 2 RZ-2014