PDBe 3mzw

X-ray diffraction
2.9Å resolution

HER2 extracelluar region with affinity matured 3-helix affibody ZHER2:342

Released:
Primary publication:
Structural basis for high-affinity HER2 receptor binding by an engineered protein.
Proc. Natl. Acad. Sci. U.S.A. 107 15039-44 (2010)
PMID: 20696930

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Immunoglobulin G-binding protein A Chain: B
Molecule details ›
Chain: B
Length: 58 amino acids
Theoretical weight: 6.71 KDa
Source organism: Staphylococcus aureus
Expression system: Not provided
UniProt:
  • Canonical: P38507 (Residues: 212-269; Coverage: 12%)
Gene name: spa
Sequence domains: B domain
Structure domains: Immunoglobulin FC, subunit C
Receptor tyrosine-protein kinase erbB-2 Chain: A
Molecule details ›
Chain: A
Length: 624 amino acids
Theoretical weight: 68.79 KDa
Source organism: Homo sapiens
Expression system: Cricetulus griseus
UniProt:
  • Canonical: P04626 (Residues: 23-646; Coverage: 51%)
Gene names: ERBB2, HER2, MLN19, NEU, NGL
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL11-1, ESRF BEAMLINE ID23-2
Spacegroup: P212121
Unit cell:
a: 71.726Å b: 97.841Å c: 148.283Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.208 0.204 0.278
Expression systems:
  • Not provided
  • Cricetulus griseus