5k0x

X-ray diffraction
2.23Å resolution

Crystal structure of the catalytic domain of the proto-oncogene tyrosine-protein kinase MER in complex with inhibitor UNC2541

Released:

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tyrosine-protein kinase Mer Chains: A, B
Molecule details ›
Chains: A, B
Length: 313 amino acids
Theoretical weight: 35.89 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q12866 (Residues: 570-864; Coverage: 30%)
Gene names: MER, MERTK
Sequence domains: Protein tyrosine kinase
Structure domains: Transferase(Phosphotransferase) domain 1

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-BM
Spacegroup: P21
Unit cell:
a: 51.671Å b: 91.599Å c: 69.769Å
α: 90° β: 102.37° γ: 90°
R-values:
R R work R free
0.189 0.185 0.239
Expression system: Escherichia coli