5utk

X-ray diffraction
2.5Å resolution

Crystal structure of the membrane proximal three fibronectin type III (FNIII) domains of Tie2 (Tie2[FNIIIa-c])

Released:
Source organism: Homo sapiens
Primary publication:
Dimerization of Tie2 mediated by its membrane-proximal FNIII domains.
Proc. Natl. Acad. Sci. U.S.A. (2017)
PMID: 28396397

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)
PDBe Complex ID:
PDB-CPX-169752 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Angiopoietin-1 receptor Chains: A, B
Molecule details ›
Chains: A, B
Length: 304 amino acids
Theoretical weight: 34.14 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: Q02763 (Residues: 442-741; Coverage: 27%)
Gene names: TEK, TIE2, VMCM, VMCM1
Sequence domains: Fibronectin type III domain

Ligands and Environments

No bound ligands
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-B
Spacegroup: C2
Unit cell:
a: 174.95Å b: 52.026Å c: 111.427Å
α: 90° β: 117.49° γ: 90°
R-values:
R R work R free
0.227 0.225 0.247
Expression system: Spodoptera frugiperda