› 5td2

X-ray diffraction
2.68Å resolution

Structure-based optimization of 1H-imidazole-2-carboxamides as Axl kinase inhibitors utilizing a Mer mutant surrogate

Released:
DOI: 10.2210/pdb5td2/pdb
PDB entry 5td2 coloured by chain, front view.
PDB entry 5td2 coloured by chain, side view.
PDB entry 5td2 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure-based optimization of 1H-imidazole-2-carboxamides as Axl kinase inhibitors utilizing a Mer mutant surrogate.
Keung W, Boloor A, Brown J, Kiryanov A, Gangloff A, Lawson JD, Skene R, Hoffman I, Atienza J, Kahana J, De Jong R, Farrell P, Balakrishna D, Halkowycz P
Bioorg Med Chem Lett 27 1099-1104 (2017)
PMID: 28082036

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-171419 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tyrosine-protein kinase Mer Chains: A, B
Molecule details ›
Chains: A, B
Length: 285 amino acids
Theoretical weight: 32.82 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q12866 (Residues: 577-861; Coverage: 29%)
Gene names: MER, MERTK
Sequence domains: Protein tyrosine and serine/threonine kinase
Structure domains: Transferase(Phosphotransferase) domain 1

Ligands and Environments

1 bound ligand:
Ligand 7AE 1 x 7AE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.3
Spacegroup: P21
Unit cell:
a: 51.157Å b: 91.942Å c: 69.655Å
α: 90° β: 99.51° γ: 90°
R-values:
R R work R free
0.251 0.248 0.3
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 citation in other articles

Structural Insights into Pseudokinase Domains of Receptor Tyrosine Kinases.
Sheetz et al. (2020)
1 more

1 mention without citation

A-loop interactions in Mer tyrosine kinase give rise to inhibitors with two-step mechanism and long residence time of binding.
Pflug et al. (2020)