› 6jxt

X-ray diffraction
2.31Å resolution

Crystal structure of EGFR 696-1022 WT in complex with AZD9291 prepared by cocrystallization

Released:
DOI: 10.2210/pdb6jxt/pdb
PDB entry 6jxt coloured by chain, front view.
PDB entry 6jxt coloured by chain, side view.
PDB entry 6jxt coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural Basis of AZD9291 Selectivity for EGFR T790M.
Yan XE, Ayaz P, Zhu SJ, Zhao P, Liang L, Zhang CH, Wu YC, Li JL, Choi HG, Huang X, Shan Y, Shaw DE, Yun CH
J Med Chem 63 8502-8511 (2020)
PMID: 32672461

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-132671 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Epidermal growth factor receptor Chain: A
Molecule details ›
Chain: A
Length: 331 amino acids
Theoretical weight: 37.45 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P00533 (Residues: 696-1022; Coverage: 28%)
Gene names: EGFR, ERBB, ERBB1, HER1
Sequence domains: Protein tyrosine and serine/threonine kinase

Ligands and Environments

2 bound ligands:
Ligand YY3 1 x YY3
Ligand CL 1 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL18U1
Spacegroup: P3221
Unit cell:
a: 86.749Å b: 86.749Å c: 103.939Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.218 0.216 0.239
Expression system: Spodoptera frugiperda

Quick links

Citations

7 review citations

Acquired resistance to third-generation EGFR-TKIs and emerging next-generation EGFR inhibitors.
Du et al. (2021)
6 more

9 mentions without citation

An overview of kinase downregulators and recent advances in discovery approaches.
Wang et al. (2021)
8 more