7len

X-ray diffraction
2.9Å resolution

Crystal structure of the epidermal growth factor receptor extracellular region with R84K mutation in complex with epiregulin crystallized with trehalose

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 dimer (preferred)
PDBe Complex ID:
PDB-CPX-127217 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (6 distinct):
Epidermal growth factor receptor Chains: A, B
Molecule details ›
Chains: A, B
Length: 507 amino acids
Theoretical weight: 56.49 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: C, D
Molecule details ›
Chains: C, D
Length: 48 amino acids
Theoretical weight: 5.48 KDa
Source organism: Homo sapiens
Expression system: Drosophila melanogaster
UniProt:
  • Canonical: O14944 (Residues: 63-110; Coverage: 34%)
Gene name: EREG

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-B
Spacegroup: P212121
Unit cell:
a: 77.737Å b: 86.6Å c: 197.795Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.24 0.237 0.295
Expression systems:
  • Spodoptera frugiperda
  • Drosophila melanogaster