PDBe 3bpr

X-ray diffraction
2.8Å resolution

Crystal structure of catalytic domain of the proto-oncogene tyrosine-protein kinase MER in complex with inhibitor C52

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, C, D
Molecule details ›
Chains: A, B, C, D
Length: 313 amino acids
Theoretical weight: 35.89 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q12866 (Residues: 570-864; Coverage: 30%)
Gene names: MER, MERTK
Sequence domains: Protein tyrosine kinase
Structure domains:

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: P21
Unit cell:
a: 70.001Å b: 91.702Å c: 120.745Å
α: 90° β: 94.06° γ: 90°
R-values:
R R work R free
0.275 0.274 0.301
Expression system: Escherichia coli BL21(DE3)