› 4p5z

X-ray diffraction
2Å resolution

Human EphA3 Kinase domain in complex with quinoxaline derivatives

Released:
DOI: 10.2210/pdb4p5z/pdb
PDB entry 4p5z coloured by chain, front view.
PDB entry 4p5z coloured by chain, side view.
PDB entry 4p5z coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Pyrrolo[3,2-b]quinoxaline derivatives as types I1/2 and II Eph tyrosine kinase inhibitors: structure-based design, synthesis, and in vivo validation.
Unzue A, Dong J, Lafleur K, Zhao H, Frugier E, Caflisch A, Nevado C
J Med Chem 57 6834-44 (2014)
PMID: 25076195

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-151400 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ephrin type-A receptor 3 Chain: A
Molecule details ›
Chain: A
Length: 361 amino acids
Theoretical weight: 40.46 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P29320 (Residues: 606-947; Coverage: 36%)
Gene names: EPHA3, ETK, ETK1, HEK, TYRO4
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand Q7M 1 x Q7M
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P21
Unit cell:
a: 52.805Å b: 38.235Å c: 75.465Å
α: 90° β: 101.46° γ: 90°
R-values:
R R work R free
0.18 0.178 0.218
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Quinoxaline-Based Scaffolds Targeting Tyrosine Kinases and Their Potential Anticancer Activity.
El Newahie et al. (2016)
7 other articles

2 mentions without citation

Structural Analysis of the Binding of Type I, I1/2, and II Inhibitors to Eph Tyrosine Kinases.
Dong et al. (2015)
1 more