› 2j5e

X-ray diffraction
3.1Å resolution

Crystal structure of EGFR kinase domain in complex with an irreversible inhibitor 13-jab

Released:
DOI: 10.2210/pdb2j5e/pdb
PDB entry 2j5e coloured by chain, front view.
PDB entry 2j5e coloured by chain, side view.
PDB entry 2j5e coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure-guided development of affinity probes for tyrosine kinases using chemical genetics.
Blair JA, Rauh D, Kung C, Yun CH, Fan QW, Rode H, Zhang C, Eck MJ, Weiss WA, Shokat KM
Nat Chem Biol 3 229-38 (2007)
PMID: 17334377

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: 327 amino acids
Theoretical weight: 37.59 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 CL 1 x CL
1 modified residue:
Ligand CY0 1 x CY0

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: I23
Unit cell:
a: 145.021Å b: 145.021Å c: 145.021Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.191 0.186 0.255
Expression system: Spodoptera frugiperda

Quick links

Citations

20 review citations

Activity-based protein profiling: from enzyme chemistry to proteomic chemistry.
Cravatt et al. (2008)
19 more

3 mentions without citation

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