› 5ia1

X-ray diffraction
2.04Å resolution

Crystal Structure of Ephrin A2 (EphA2) Receptor Protein Kinase with MLN8054

Released:
DOI: 10.2210/pdb5ia1/pdb
PDB entry 5ia1 coloured by chain, front view.
PDB entry 5ia1 coloured by chain, side view.
PDB entry 5ia1 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 ZZL 1 x ZZL
Ligand EDO 1 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: 32.714Å b: 106.741Å c: 40.729Å
α: 90° β: 108.79° γ: 90°
R-values:
R R work R free
0.183 0.181 0.223
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