› 1nql

X-ray diffraction
2.8Å resolution

Structure of the extracellular domain of human epidermal growth factor (EGF) receptor in an inactive (low pH) complex with EGF.

Released:
DOI: 10.2210/pdb1nql/pdb
PDB entry 1nql coloured by chain, front view.
PDB entry 1nql coloured by chain, side view.
PDB entry 1nql coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
EGF activates its receptor by removing interactions that autoinhibit ectodomain dimerization.
Ferguson KM, Berger MB, Mendrola JM, Cho HS, Leahy DJ, Lemmon MA
Mol Cell 11 507-17 (2003)
PMID: 12620237

Function and Biology Details

Reaction catalysed: 
ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132672 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (4 distinct):
Epidermal growth factor receptor Chain: A
Molecule details ›
Chain: A
Length: 624 amino acids
Theoretical weight: 69.21 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P00533 (Residues: 25-642; Coverage: 52%)
Gene names: EGFR, ERBB, ERBB1, HER1
Sequence domains:
Structure domains:
Epidermal growth factor Chain: B
Molecule details ›
Chain: B
Length: 53 amino acids
Theoretical weight: 6.23 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P01133 (Residues: 971-1023; Coverage: 5%)
Gene name: EGF
Sequence domains: EGF-like domain
Structure domains: Laminin

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, BMA
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer
1 bound ligand:
Ligand NAG 5 x NAG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE F1
Spacegroup: C2
Unit cell:
a: 119.17Å b: 103.66Å c: 101.49Å
α: 90° β: 119.27° γ: 90°
R-values:
R R work R free
0.247 0.241 0.31
Expression systems:
  • Spodoptera frugiperda
  • Escherichia coli

Quick links

Citations

106 review citations

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

79 mentions without citation

Receptor tyrosine kinases: mechanisms of activation and signaling.
Hubbard et al. (2007)
78 more