PDBe 5n06

X-ray diffraction
2.5Å resolution

Crystal structure of Tie1 Fibronectin-like domain 3

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:
Tyrosine-protein kinase receptor Tie-1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 126 amino acids
Theoretical weight: 14.07 KDa
Source organism: Homo sapiens
Expression system: Spodoptera aff. frugiperda 2 RZ-2014
UniProt:
  • Canonical: P35590 (Residues: 639-738; Coverage: 9%)
Gene names: TIE, TIE1
Sequence domains: Fibronectin type III domain

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P65
Unit cell:
a: 54.054Å b: 54.054Å c: 107.27Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.249 0.244 0.315
Expression system: Spodoptera aff. frugiperda 2 RZ-2014