› 2yn8

X-ray diffraction
2.11Å resolution

ephB4 kinase domain inhibitor complex

Released:
DOI: 10.2210/pdb2yn8/pdb
PDB entry 2yn8 coloured by chain, front view.
PDB entry 2yn8 coloured by chain, side view.
PDB entry 2yn8 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Stability and solubility engineering of the EphB4 tyrosine kinase catalytic domain using a rationally designed synthetic library.
Overman RC, Green I, Truman CM, Read JA, Embrey KJ, McAlister MS, Attwood TK
Protein Eng Des Sel 26 695-704 (2013)
PMID: 23840071

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 Chains: A, B
Molecule details ›
Chains: A, B
Length: 298 amino acids
Theoretical weight: 33.53 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
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

1 bound ligand:
Ligand STU 2 x STU
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E
Spacegroup: P21
Unit cell:
a: 51.635Å b: 89.527Å c: 81.087Å
α: 90° β: 103.21° γ: 90°
R-values:
R R work R free
0.197 0.195 0.234
Expression system: Spodoptera frugiperda

Quick links

Citations

1 citations in other articles

Identification and regulation of the catalytic promiscuity of (-)-γ-lactamase from Microbacterium hydrocarbonoxydans.
Sun et al. (2015)

1 mention without citation

Stability and solubility engineering of the EphB4 tyrosine kinase catalytic domain using a rationally designed synthetic library.
Overman et al. (2013)