› 1ivo

X-ray diffraction
3.3Å resolution

Crystal Structure of the Complex of Human Epidermal Growth Factor and Receptor Extracellular Domains.

Released:
DOI: 10.2210/pdb1ivo/pdb
PDB entry 1ivo coloured by chain, front view.
PDB entry 1ivo coloured by chain, side view.
PDB entry 1ivo coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure of the complex of human epidermal growth factor and receptor extracellular domains.
Ogiso H, Ishitani R, Nureki O, Fukai S, Yamanaka M, Kim JH, Saito K, Sakamoto A, Inoue M, Shirouzu M, Yokoyama S
Cell 110 775-87 (2002)
PMID: 12297050

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 tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132702 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (3 distinct):
Epidermal growth factor receptor Chains: A, B
Molecule details ›
Chains: A, B
Length: 622 amino acids
Theoretical weight: 68.78 KDa
Source organism: Homo sapiens
Expression system: Cricetulus griseus
UniProt:
  • Canonical: P00533 (Residues: 25-646; Coverage: 52%)
Gene names: EGFR, ERBB, ERBB1, HER1
Sequence domains:
Structure domains:
Epidermal growth factor Chains: C, D
Molecule details ›
Chains: C, D
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
Carbohydrate polymer
1 bound ligand:
Ligand NAG 8 x NAG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL41XU
Spacegroup: P3121
Unit cell:
a: 220.164Å b: 220.164Å c: 113.121Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.258 0.255 0.326
Expression systems:
  • Cricetulus griseus
  • Escherichia coli

Quick links

Citations

163 review citations

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

93 mentions without citation

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