› 6fnl

X-ray diffraction
1.27Å resolution

Crystal Structure of Ephrin B4 (EphB4) Receptor Protein Kinase

Released:
DOI: 10.2210/pdb6fnl/pdb
PDB entry 6fnl coloured by chain, front view.
PDB entry 6fnl coloured by chain, side view.
PDB entry 6fnl coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
NVP-BHG712: Effects of Regioisomers on the Affinity and Selectivity toward the EPHrin Family.
Tröster A, Heinzlmeir S, Berger BT, Gande SL, Saxena K, Sreeramulu S, Linhard V, Nasiri AH, Bolte M, Müller S, Kuster B, Médard G, Kudlinzki D, Schwalbe H
ChemMedChem 13 1629-1633 (2018)
PMID: 29928781

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: 297 amino acids
Theoretical weight: 33.49 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P54760 (Residues: 598-892; Coverage: 30%)
Gene names: EPHB4, HTK, MYK1, TYRO11
Sequence domains: Protein tyrosine and serine/threonine kinase
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: P21
Unit cell:
a: 46.138Å b: 54.061Å c: 62.119Å
α: 90° β: 110.87° γ: 90°
R-values:
R R work R free
0.197 0.196 0.214
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

EphrinB2-EphB4 Signaling in Neurooncological Disease.
Piffko et al. (2022)
1 more

1 mention without citation

An investigation of binding interactions of tumor-targeted peptide conjugated polyphenols with the kinase domain of ephrin B4 and B2 receptors.
Mitchell et al. (2023)