› 5i9w

X-ray diffraction
1.36Å resolution

Crystal Structure of Ephrin A2 (EphA2) Receptor Protein Kinase with ANP

Released:
DOI: 10.2210/pdb5i9w/pdb
PDB entry 5i9w coloured by chain, front view.
PDB entry 5i9w coloured by chain, side view.
PDB entry 5i9w coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Chemical Proteomics and Structural Biology Define EPHA2 Inhibition by Clinical Kinase Drugs.
Heinzlmeir S, Kudlinzki D, Sreeramulu S, Klaeger S, Gande SL, Linhard V, Wilhelm M, Qiao H, Helm D, Ruprecht B, Saxena K, Médard G, Schwalbe H, Kuster B
ACS Chem Biol 11 3400-3411 (2016)
PMID: 27768280

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

2 bound ligands:
Ligand ANP 1 x ANP
Ligand EDO 2 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PETRA III, EMBL c/o DESY BEAMLINE P13 (MX1)
Spacegroup: P21
Unit cell:
a: 32.733Å b: 107.547Å c: 40.479Å
α: 90° β: 108.77° γ: 90°
R-values:
R R work R free
0.17 0.17 0.18
Expression system: Spodoptera frugiperda

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Citations

7 review citations

Oncogenic functions and therapeutic targeting of EphA2 in cancer.
Wilson et al. (2021)
6 more