› 2p0c

X-ray diffraction
2.4Å resolution

Catalytic Domain of the Proto-oncogene Tyrosine-protein Kinase MER

Released:
DOI: 10.2210/pdb2p0c/pdb
PDB entry 2p0c coloured by chain, front view.
PDB entry 2p0c coloured by chain, side view.
PDB entry 2p0c coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural insights into the inhibited states of the Mer receptor tyrosine kinase.
Huang X, Finerty P, Walker JR, Butler-Cole C, Vedadi M, Schapira M, Parker SA, Turk BE, Thompson DA, Dhe-Paganon S
J Struct Biol 165 88-96 (2009)
PMID: 19028587

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: 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 and serine/threonine kinase
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand MG 3 x MG
Ligand ANP 2 x ANP
Ligand BME 1 x BME
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P21
Unit cell:
a: 52.47Å b: 90.057Å c: 69.253Å
α: 90° β: 102.44° γ: 90°
R-values:
R R work R free
0.208 0.204 0.274
Expression system: Escherichia coli

Quick links

Citations

8 review citations

Biology of the TAM receptors.
Lemke G. (2013)
7 more

6 mentions without citation

Structural insights into the inhibited states of the Mer receptor tyrosine kinase.
Huang et al. (2009)
5 more