› 2ivu

X-ray diffraction
2.5Å resolution

Crystal structure of phosphorylated RET tyrosine kinase domain complexed with the inhibitor ZD6474

Released:
DOI: 10.2210/pdb2ivu/pdb
PDB entry 2ivu coloured by chain, front view.
PDB entry 2ivu coloured by chain, side view.
PDB entry 2ivu coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure and chemical inhibition of the RET tyrosine kinase domain.
Knowles PP, Murray-Rust J, Kjaer S, Scott RP, Hanrahan S, Santoro M, Ibáñez CF, McDonald NQ
J Biol Chem 281 33577-87 (2006)
PMID: 16928683

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 2 x FMT
Ligand ZD6 1 x ZD6
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: 71.409Å b: 71.42Å c: 78.834Å
α: 90° β: 101.23° γ: 90°
R-values:
R R work R free
0.193 0.19 0.248
Expression system: Spodoptera frugiperda

Quick links

Citations

62 review citations

Cell signaling by receptor tyrosine kinases.
Lemmon et al. (2010)
61 more

32 mentions without citation

Precision therapy for RET-altered cancers with RET inhibitors.
Thein et al. (2021)
31 more