› 7ab0

X-ray diffraction
1.74Å resolution

Apo crystal structure of the MerTK kinase domain

Released:
DOI: 10.2210/pdb7ab0/pdb
PDB entry 7ab0 coloured by chain, front view.
PDB entry 7ab0 coloured by chain, side view.
PDB entry 7ab0 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
A-loop interactions in Mer tyrosine kinase give rise to inhibitors with two-step mechanism and long residence time of binding.
Pflug A, Schimpl M, Nissink JWM, Overman RC, Rawlins PB, Truman C, Underwood E, Warwicker J, Winter-Holt J, McCoull W
Biochem J 477 4443-4452 (2020)
PMID: 33119085

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 Chain: A
Molecule details ›
Chain: A
Length: 298 amino acids
Theoretical weight: 34.38 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q12866 (Residues: 571-864; Coverage: 30%)
Gene names: MER, MERTK
Sequence domains: Protein tyrosine and serine/threonine kinase

Ligands and Environments

1 bound ligand:
Ligand CL 5 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: C2221
Unit cell:
a: 91.621Å b: 91.604Å c: 71.623Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.202 0.2 0.246
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 citations in other articles

BMS794833 inhibits macrophage efferocytosis by directly binding to MERTK and inhibiting its activity.
Bae et al. (2022)

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)