› 3eoa

X-ray diffraction
2.8Å resolution

Crystal structure the Fab fragment of Efalizumab in complex with LFA-1 I domain, Form I

Released:
DOI: 10.2210/pdb3eoa/pdb
PDB entry 3eoa coloured by chain, front view.
PDB entry 3eoa coloured by chain, side view.
PDB entry 3eoa coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Efalizumab binding to the LFA-1 alphaL I domain blocks ICAM-1 binding via steric hindrance.
Li S, Wang H, Peng B, Zhang M, Zhang D, Hou S, Guo Y, Ding J
Proc Natl Acad Sci U S A 106 4349-54 (2009)
PMID: 19258452

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-233999 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Efalizumab Fab fragment, light chain Chains: A, L
Molecule details ›
Chains: A, 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 Chains: B, H
Molecule details ›
Chains: B, H
Length: 220 amino acids
Theoretical weight: 23.75 KDa
Source organism: Homo sapiens
Expression system: Not provided
Structure domains: Immunoglobulins
Integrin alpha-L Chains: I, J
Molecule details ›
Chains: I, J
Length: 181 amino acids
Theoretical weight: 20.68 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P20701 (Residues: 153-333; Coverage: 16%)
Gene names: CD11A, ITGAL
Sequence domains: von Willebrand factor type A domain
Structure domains: von Willebrand factor, type A domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE AR-NW12A
Spacegroup: P212121
Unit cell:
a: 64.719Å b: 81.696Å c: 281.882Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.227 0.225 0.264
Expression systems:
  • Not provided
  • Escherichia coli

Quick links

Citations

5 review citations

Integrins as therapeutic targets: lessons and opportunities.
Cox et al. (2010)
4 more

10 mentions without citation

Updates to the Integrated Protein-Protein Interaction Benchmarks: Docking Benchmark Version 5 and Affinity Benchmark Version 2.
Vreven et al. (2015)
9 more