Structure analysis

Crystal Structure of EGFR-WT in Complex with TAK-788

X-ray diffraction
2.5Å resolution
Source organism: Homo sapiens
Assembly composition:
monomeric (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: monomeric
Accessible surface area: 14556.68 Å2
Buried surface area: 279.39 Å2
Dissociation area: 139.69 Å2
Dissociation energy (ΔGdiss): -4.25 kcal/mol
Dissociation entropy (TΔSdiss): 2.79 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-132671

Macromolecules

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
Pfam: Protein tyrosine and serine/threonine kinase
InterPro:

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