› 4aw5

X-ray diffraction
2.33Å resolution

Complex of the EphB4 kinase domain with an oxindole inhibitor

Released:
DOI: 10.2210/pdb4aw5/pdb
PDB entry 4aw5 coloured by chain, front view.
PDB entry 4aw5 coloured by chain, side view.
PDB entry 4aw5 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The design, synthesis, and biological evaluation of potent receptor tyrosine kinase inhibitors.
Kim MH, Tsuhako AL, Co EW, Aftab DT, Bentzien F, Chen J, Cheng W, Engst S, Goon L, Klein RR, Le DT, Mac M, Parks JJ, Qian F, Rodriquez M, Stout TJ, Till JH, Won KA, Wu X, Yakes FM, Yu P, Zhang W, Zhao Y, Lamb P, Nuss JM, Xu W
Bioorg Med Chem Lett 22 4979-85 (2012)
PMID: 22765894

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-157090 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ephrin type-B receptor 4 Chain: A
Molecule details ›
Chain: A
Length: 291 amino acids
Theoretical weight: 32.9 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P54760 (Residues: 605-890; Coverage: 29%)
Gene names: EPHB4, HTK, MYK1, TYRO11
Sequence domains: Protein tyrosine and serine/threonine kinase
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand 30K 1 x 30K
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 32-ID
Spacegroup: P21
Unit cell:
a: 46.657Å b: 53.978Å c: 63.242Å
α: 90° β: 111.06° γ: 90°
R-values:
R R work R free
0.194 0.19 0.279
Expression system: Spodoptera frugiperda

Quick links

Citations

2 review citations

Oxindole: A chemical prism carrying plethora of therapeutic benefits.
Kaur et al. (2016)
1 more

3 mentions without citation

StructMAn: annotation of single-nucleotide polymorphisms in the structural context.
Gress et al. (2016)
2 more