› 5gty

X-ray diffraction
3.14Å resolution

Crystal structure of EGFR 696-1022 T790M in complex with LXX-6-26

Released:
DOI: 10.2210/pdb5gty/pdb
PDB entry 5gty coloured by chain, front view.
PDB entry 5gty coloured by chain, side view.
PDB entry 5gty coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Discovery and characterization of a novel irreversible EGFR mutants selective and potent kinase inhibitor CHMFL-EGFR-26 with a distinct binding mode.
Hu C, Wang A, Wu H, Qi Z, Li X, Yan XE, Chen C, Yu K, Zou F, Wang W, Wang W, Wu J, Liu J, Wang B, Wang L, Ren T, Zhang S, Yun CH, Liu J, Liu Q
Oncotarget 8 18359-18372 (2017)
PMID: 28407693

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 tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132708 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Epidermal growth factor receptor Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 331 amino acids
Theoretical weight: 37.65 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
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand 816 8 x 816
Ligand EDO 4 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL19U1
Spacegroup: P21
Unit cell:
a: 117.427Å b: 71.796Å c: 152.53Å
α: 90° β: 103.53° γ: 90°
R-values:
R R work R free
0.258 0.257 0.28
Expression system: Spodoptera frugiperda

Quick links

Citations

1 review citation

Toward structure-based drug design against the epidermal growth factor receptor (EGFR).
Haddad et al. (2021)
2 other articles

13 mentions without citation

Discovery and characterization of a novel irreversible EGFR mutants selective and potent kinase inhibitor CHMFL-EGFR-26 with a distinct binding mode.
Hu et al. (2017)
12 more