5wb7

X-ray diffraction
2.94Å resolution

Crystal structure of the epidermal growth factor receptor extracellular region in complex with epiregulin

Released:

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

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
PDBe Complex ID:
PDB-CPX-127220 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (6 distinct):
Epidermal growth factor receptor Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 507 amino acids
Theoretical weight: 56.52 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P00533 (Residues: 25-525; Coverage: 42%)
Gene names: EGFR, ERBB, ERBB1, HER1
Sequence domains:
Epiregulin Chains: E, F, G, H
Molecule details ›
Chains: E, F, G, H
Length: 62 amino acids
Theoretical weight: 7.04 KDa
Source organism: Homo sapiens
Expression system: Drosophila melanogaster
UniProt:
  • Canonical: O14944 (Residues: 56-116; Coverage: 44%)
Gene name: EREG
Structure domains: Laminin

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, BMA, MAN
Carbohydrate polymer : NEW Components: NAG, BMA, MAN
Carbohydrate polymer : NEW Components: NAG, BMA
Carbohydrate polymer : NEW Components: NAG
1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-D
Spacegroup: P21
Unit cell:
a: 76.647Å b: 199.288Å c: 87.916Å
α: 90° β: 96.74° γ: 90°
R-values:
R R work R free
0.227 0.225 0.268
Expression systems:
  • Spodoptera frugiperda
  • Drosophila melanogaster