› 3b8q

X-ray diffraction
2.75Å resolution

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
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-153084 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Vascular endothelial growth factor receptor 2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 314 amino acids
Theoretical weight: 36.28 KDa
Source organism: Homo sapiens
Expression system: Trichoplusia ni
UniProt:
  • Canonical: P35968 (Residues: 815-1171; Coverage: 23%)
Gene names: FLK1, KDR, VEGFR2
Sequence domains: Protein tyrosine and serine/threonine kinase
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand 900 2 x 900
1 modified residue:
Ligand PTR 4 x PTR

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.2
Spacegroup: P21
Unit cell:
a: 55.116Å b: 67.782Å c: 88.089Å
α: 90° β: 92.137° γ: 90°
R-values:
R R work R free
0.218 0.218 0.276
Expression system: Trichoplusia ni

Quick links

Citations

1 review citation

Update on lymphocyte specific kinase inhibitors: a patent survey.
Martin et al. (2010)
22 other articles

6 mentions without citation

Novel VEGFR-2 kinase inhibitors identified by the back-to-front approach.
Sanphanya et al. (2013)
5 more