› 4hjo

X-ray diffraction
2.75Å resolution

Crystal structure of the inactive EGFR tyrosine kinase domain with erlotinib

Released:
DOI: 10.2210/pdb4hjo/pdb
PDB entry 4hjo coloured by chain, front view.
PDB entry 4hjo coloured by chain, side view.
PDB entry 4hjo coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Erlotinib binds both inactive and active conformations of the EGFR tyrosine kinase domain.
Park JH, Liu Y, Lemmon MA, Radhakrishnan R
OpenAccess logo Biochem J 448 417-23 (2012)
PMID: 23101586

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: 337 amino acids
Theoretical weight: 38.56 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

1 bound ligand:
Ligand AQ4 1 x AQ4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-D
Spacegroup: C2221
Unit cell:
a: 77.967Å b: 114.284Å c: 84.918Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.231 0.23 0.253
Expression system: Spodoptera frugiperda

Quick links

Citations

8 review citations

A structural perspective on the regulation of the epidermal growth factor receptor.
Kovacs et al. (2015)
7 more

74 mentions without citation

Personalized cancer medicine: molecular diagnostics, predictive biomarkers, and drug resistance.
Gonzalez de Castro et al. (2013)
73 more