› 5njz

X-ray diffraction
1.77Å resolution

Crystal Structure of Ephrin A2 (EphA2) Receptor Protein Kinase with Compound 1g

Released:
DOI: 10.2210/pdb5njz/pdb
PDB entry 5njz coloured by chain, front view.
PDB entry 5njz coloured by chain, side view.
PDB entry 5njz coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Chemoproteomics-Aided Medicinal Chemistry for the Discovery of EPHA2 Inhibitors.
Heinzlmeir S, Lohse J, Treiber T, Kudlinzki D, Linhard V, Gande SL, Sreeramulu S, Saxena K, Liu X, Wilhelm M, Schwalbe H, Kuster B, Médard G
ChemMedChem 12 999-1011 (2017)
PMID: 28544567

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-151387 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ephrin type-A receptor 2 Chain: A
Molecule details ›
Chain: A
Length: 306 amino acids
Theoretical weight: 34.46 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P29317 (Residues: 596-900; Coverage: 32%)
Gene names: ECK, EPHA2
Sequence domains: Protein tyrosine and serine/threonine kinase
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand 8ZH 1 x 8ZH
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.2
Spacegroup: P21
Unit cell:
a: 32.697Å b: 107.256Å c: 40.466Å
α: 90° β: 108.62° γ: 90°
R-values:
R R work R free
0.165 0.163 0.199
Expression system: Spodoptera frugiperda

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Citations

8 review citations

Targeting EphA2 in cancer.
Xiao et al. (2020)
7 more