› 5e1s

X-ray diffraction
2.26Å resolution

The Crystal structure of INSR Tyrosine Kinase in complex with the Inhibitor BI 885578

Released:
DOI: 10.2210/pdb5e1s/pdb
PDB entry 5e1s coloured by chain, front view.
PDB entry 5e1s coloured by chain, side view.
PDB entry 5e1s coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
BI 885578, a Novel IGF1R/INSR Tyrosine Kinase Inhibitor with Pharmacokinetic Properties That Dissociate Antitumor Efficacy and Perturbation of Glucose Homeostasis.
Sanderson MP, Apgar J, Garin-Chesa P, Hofmann MH, Kessler D, Quant J, Savchenko A, Schaaf O, Treu M, Tye H, Zahn SK, Zoephel A, Haaksma E, Adolf GR, Kraut N
Mol Cancer Ther 14 2762-72 (2015)
PMID: 26438154

Function and Biology Details

Reaction catalysed: 
ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-138931 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Insulin receptor subunit beta Chain: A
Molecule details ›
Chain: A
Length: 308 amino acids
Theoretical weight: 34.95 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P06213 (Residues: 1005-1310; Coverage: 23%)
Gene name: INSR
Sequence domains: Protein tyrosine and serine/threonine kinase
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand 5JA 1 x 5JA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P212121
Unit cell:
a: 56.55Å b: 70.37Å c: 87.85Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.215 0.213 0.262
Expression system: Spodoptera frugiperda

Quick links

Citations

4 review citations

Insulin Receptor Isoforms in Physiology and Disease: An Updated View.
Belfiore et al. (2017)
3 more

6 mentions without citation

Automated refinement of macromolecular structures at low resolution using prior information.
Kovalevskiy et al. (2016)
5 more