› 3lzb

X-ray diffraction
2.7Å resolution

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 Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 327 amino acids
Theoretical weight: 36.14 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P00533 (Residues: 696-983; Coverage: 24%)
Gene names: EGFR, ERBB, ERBB1, HER1
Sequence domains: Protein tyrosine and serine/threonine kinase
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand ITI 4 x ITI
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-BM
Spacegroup: P21
Unit cell:
a: 85.586Å b: 70.874Å c: 115.182Å
α: 90° β: 109.36° γ: 90°
R-values:
R R work R free
0.206 0.204 0.257
Expression system: Spodoptera frugiperda

Quick links

Citations

6 review citations

New and unusual scaffolds in medicinal chemistry.
Marson CM. (2011)
5 more

8 mentions without citation

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