› 5fm3

X-ray diffraction
2.95Å resolution

Crystal structure of hyper-phosphorylated RET kinase domain with (proximal) juxtamembrane segment

Released:
DOI: 10.2210/pdb5fm3/pdb
PDB entry 5fm3 coloured by chain, front view.
PDB entry 5fm3 coloured by chain, side view.
PDB entry 5fm3 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
RET Functions as a Dual-Specificity Kinase that Requires Allosteric Inputs from Juxtamembrane Elements.
Plaza-Menacho I, Barnouin K, Barry R, Borg A, Orme M, Chauhan R, Mouilleron S, Martínez-Torres RJ, Meier P, McDonald NQ
Cell Rep 17 3319-3332 (2016)
PMID: 28009299

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: 355 amino acids
Theoretical weight: 40.72 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P07949 (Residues: 659-1013; Coverage: 33%)
Gene names: CDHF12, CDHR16, PTC, RET
Sequence domains: Protein tyrosine and serine/threonine kinase
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand PP1 1 x PP1
2 modified residues:
Ligand PTR 3 x PTR
Ligand SEP 1 x SEP

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I24
Spacegroup: P6322
Unit cell:
a: 98.569Å b: 98.569Å c: 146.301Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.2 0.199 0.224
Expression system: Spodoptera frugiperda

Quick links

Citations

8 review citations

RET Receptor Tyrosine Kinase: Role in Neurodegeneration, Obesity, and Cancer.
Mahato et al. (2020)
7 more

3 mentions without citation

Leveraging Atropisomerism to Obtain a Selective Inhibitor of RET Kinase with Secondary Activities toward EGFR Mutants.
Toenjes et al. (2019)
2 more