3eo9

X-ray diffraction
1.8Å resolution

Crystal structure the Fab fragment of Efalizumab

Released:
Source organism: Homo sapiens
Primary publication:
Efalizumab binding to the LFA-1 alphaL I domain blocks ICAM-1 binding via steric hindrance.
Proc Natl Acad Sci U S A 106 4349-54 (2009)
PMID: 19258452

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-234862 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Efalizumab Fab fragment, light chain Chain: L
Molecule details ›
Chain: L
Length: 214 amino acids
Theoretical weight: 23.44 KDa
Source organism: Homo sapiens
Expression system: Not provided
Structure domains: Immunoglobulins
Efalizumab Fab fragment, heavy chain Chain: H
Molecule details ›
Chain: H
Length: 219 amino acids
Theoretical weight: 23.62 KDa
Source organism: Homo sapiens
Expression system: Not provided
Structure domains: Immunoglobulins

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P3121
Unit cell:
a: 87.198Å b: 87.198Å c: 117.223Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.191 0.189 0.217
Expression system: Not provided