3cpb

X-ray diffraction
2.7Å resolution

Crystal structure of the VEGFR2 kinase domain in complex with a bisamide inhibitor

Released:

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:
monomeric (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:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 31-ID
Spacegroup: P21
Unit cell:
a: 54.919Å b: 67.552Å c: 88.73Å
α: 90° β: 92.524° γ: 90°
R-values:
R R work R free
0.224 0.219 0.286
Expression system: Trichoplusia ni