› 2x2k

X-ray diffraction
2.6Å resolution

Crystal Structure of phosphorylated RET tyrosine kinase domain with inhibitor

Released:
DOI: 10.2210/pdb2x2k/pdb
PDB entry 2x2k coloured by chain, front view.
PDB entry 2x2k coloured by chain, side view.
PDB entry 2x2k coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Synthesis, structure-activity relationship and crystallographic studies of 3-substituted indolin-2-one RET inhibitors.
Mologni L, Rostagno R, Brussolo S, Knowles PP, Kjaer S, Murray-Rust J, Rosso E, Zambon A, Scapozza L, McDonald NQ, Lucchini V, Gambacorti-Passerini C
Bioorg Med Chem 18 1482-96 (2010)
PMID: 20117004

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:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139854 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Soluble RET kinase fragment Chain: A
Molecule details ›
Chain: A
Length: 314 amino acids
Theoretical weight: 35.79 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P07949 (Residues: 703-1013; Coverage: 29%)
Gene names: CDHF12, CDHR16, PTC, RET
Sequence domains: Protein tyrosine and serine/threonine kinase
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand FMT 3 x FMT
Ligand X2K 1 x X2K
1 modified residue:
Ligand PTR 1 x PTR

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: C2
Unit cell:
a: 71.6Å b: 70.912Å c: 78.871Å
α: 90° β: 101.68° γ: 90°
R-values:
R R work R free
0.194 0.191 0.256
Expression system: Spodoptera frugiperda

Quick links

Citations

3 review citations

Mechanisms of RET signaling in cancer: current and future implications for targeted therapy.
Plaza-Menacho et al. (2014)
2 more

4 mentions without citation

The methionine-aromatic motif plays a unique role in stabilizing protein structure.
Valley et al. (2012)
3 more