PDBe 2p4i

X-ray diffraction
2.5Å resolution

Evolution of a highly Selective and Potent 2-(Pyridin-2-yl)-1,3,5-triazine Tie-2 Kinase Inhibitor

Released:

Function and Biology Details

Reaction catalysed:
ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate. 
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Angiopoietin-1 receptor Chains: A, B
Molecule details ›
Chains: A, B
Length: 317 amino acids
Theoretical weight: 36.25 KDa
Source organism: Homo sapiens
Expression system: Trichoplusia ni
UniProt:
  • Canonical: Q02763 (Residues: 808-1124; Coverage: 29%)
Gene names: TEK, TIE2, VMCM, VMCM1
Sequence domains: Protein tyrosine kinase
Structure domains:

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P212121
Unit cell:
a: 64.262Å b: 63.189Å c: 175.571Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.248 0.246 0.303
Expression system: Trichoplusia ni