X-ray diffraction
1.25Å resolution

The Structure of ERBIN PDZ domain bound to the Carboxy-terminal tail of the ErbB2 Receptor

Source organism: Homo sapiens
Primary publication:
Novel mode of ligand recognition by the Erbin PDZ domain.
J. Biol. Chem. 278 1399-402 (2003)
PMID: 12444095

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Erbin Chain: A
Molecule details ›
Chain: A
Length: 95 amino acids
Theoretical weight: 10.29 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
  • Canonical: Q96RT1 (Residues: 1321-1412; Coverage: 7%)
Gene names: ERBB2IP, ERBIN, KIAA1225, LAP2
Sequence domains: PDZ domain
Structure domains: Pdz3 Domain
Receptor tyrosine-protein kinase erbB-2 Chain: B
Molecule details ›
Chain: B
Length: 9 amino acids
Theoretical weight: 1 KDa
Source organism: Homo sapiens
Expression system: Not provided
  • Canonical: P04626 (Residues: 1247-1255; Coverage: 1%)
Gene names: ERBB2, HER2, MLN19, NEU, NGL

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE F2
Spacegroup: P21
Unit cell:
a: 26.605Å b: 57.417Å c: 30.439Å
α: 90° β: 100.59° γ: 90°
R R work R free
0.13 0.128 0.165
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided