› 1m17

X-ray diffraction
2.6Å resolution

Epidermal Growth Factor Receptor tyrosine kinase domain with 4-anilinoquinazoline inhibitor erlotinib

Released:
DOI: 10.2210/pdb1m17/pdb
PDB entry 1m17 coloured by chain, front view.
PDB entry 1m17 coloured by chain, side view.
PDB entry 1m17 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure of the epidermal growth factor receptor kinase domain alone and in complex with a 4-anilinoquinazoline inhibitor.
Stamos J, Sliwkowski MX, Eigenbrot C
J Biol Chem 277 46265-72 (2002)
PMID: 12196540

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 domain:

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: 333 amino acids
Theoretical weight: 37.88 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P00533 (Residues: 695-1022; 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: ALS BEAMLINE 5.0.1
Spacegroup: I23
Unit cell:
a: 147.8Å b: 147.8Å c: 147.8Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.253 0.251 0.295
Expression system: Spodoptera frugiperda

Quick links

Citations

102 review citations

Regulation of protein kinases; controlling activity through activation segment conformation.
Nolen et al. (2004)
101 more

359 mentions without citation

Structure and clinical relevance of the epidermal growth factor receptor in human cancer.
Kumar et al. (2008)
358 more