› 2gs2

X-ray diffraction
2.8Å resolution

Crystal Structure of the active EGFR kinase domain

Released:
DOI: 10.2210/pdb2gs2/pdb
PDB entry 2gs2 coloured by chain, front view.
PDB entry 2gs2 coloured by chain, side view.
PDB entry 2gs2 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
An allosteric mechanism for activation of the kinase domain of epidermal growth factor receptor.
Zhang X, Gureasko J, Shen K, Cole PA, Kuriyan J
Cell 125 1137-49 (2006)
PMID: 16777603

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:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132701 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Epidermal growth factor receptor Chain: A
Molecule details ›
Chain: A
Length: 330 amino acids
Theoretical weight: 37.56 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

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.3.1
Spacegroup: I23
Unit cell:
a: 145.543Å b: 145.543Å c: 145.543Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.248 0.205 0.25
Expression system: Spodoptera frugiperda

Quick links

Citations

270 review citations

Cell signaling by receptor tyrosine kinases.
Lemmon et al. (2010)
269 more

46 mentions without citation

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