› 6ne7

X-ray diffraction
1.99Å resolution

Structure of G810A mutant of RET protein tyrosine kinase domain.

Released:
DOI: 10.2210/pdb6ne7/pdb
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PDB entry 6ne7 coloured by chain, front view.
PDB entry 6ne7 coloured by chain, side view.
PDB entry 6ne7 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis of resistance of mutant RET protein-tyrosine kinase to its inhibitors nintedanib and vandetanib.
Terzyan SS, Shen T, Liu X, Huang Q, Teng P, Zhou M, Hilberg F, Cai J, Mooers BHM, Wu J
J Biol Chem 294 10428-10437 (2019)
PMID: 31118272

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-139853 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Soluble RET kinase fragment Chain: A
Molecule details ›
Chain: A
Length: 314 amino acids
Theoretical weight: 35.88 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P07949 (Residues: 705-1013; Coverage: 29%)
Gene names: CDHF12, CDHR16, PTC, RET
Sequence domains: Protein tyrosine and serine/threonine kinase

Ligands and Environments

2 bound ligands:
Ligand FMT 2 x FMT
Ligand AMP 1 x AMP
1 modified residue:
Ligand PTR 2 x PTR

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: SSRL BEAMLINE BL14-1
Spacegroup: C2
Unit cell:
a: 72.286Å b: 69.858Å c: 78.971Å
α: 90° β: 102.26° γ: 90°
R-values:
R R work R free
0.206 0.203 0.249
Expression system: Spodoptera frugiperda

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Citations

15 review citations

Advances in Targeting RET-Dependent Cancers.
Subbiah et al. (2020)
14 more

1 mention without citation

Structural basis of resistance of mutant RET protein-tyrosine kinase to its inhibitors nintedanib and vandetanib.
Terzyan et al. (2019)

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