› 1bbj

X-ray diffraction
3.1Å resolution

CRYSTAL STRUCTURE OF A CHIMERIC FAB' FRAGMENT OF AN ANTIBODY BINDING TUMOUR CELLS

Released:
DOI: 10.2210/pdb1bbj/pdb
PDB entry 1bbj coloured by chain, front view.
PDB entry 1bbj coloured by chain, side view.
PDB entry 1bbj coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Crystal structure of a chimeric Fab' fragment of an antibody binding tumour cells.
Brady RL, Edwards DJ, Hubbard RE, Jiang JS, Lange G, Roberts SM, Todd RJ, Adair JR, Emtage JS, King DJ
J Mol Biol 227 253-64 (1992)
PMID: 1522589

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-208634 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
IGG4-KAPPA B72.3 FAB (LIGHT CHAIN) Chains: A, L
Molecule details ›
Chains: A, L
Length: 211 amino acids
Theoretical weight: 23.15 KDa
Source organism: Mus musculus
Expression system: Cricetulus griseus
Structure domains: Immunoglobulins
Immunoglobulin heavy constant gamma 4 Chains: B, H
Molecule details ›
Chains: B, H
Length: 212 amino acids
Theoretical weight: 22.79 KDa
Source organism: Mus musculus
Expression system: Cricetulus griseus
UniProt:
  • Canonical: P01861 (Residues: 1-98; Coverage: 25%)
Gene name: IGHG4
Sequence domains: Immunoglobulin C1-set domain
Structure domains: Immunoglobulins

Ligands and Environments

No bound ligands
1 modified residue:
Ligand PCA 2 x PCA

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 67.5Å b: 93.2Å c: 208.8Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.176 not available not available
Expression system: Cricetulus griseus

Quick links

Citations

5 review citations

Anatomy of the antibody molecule.
Padlan EA. (1994)
4 more

16 mentions without citation

Long lasting neutralization of C5 by SKY59, a novel recycling antibody, is a potential therapy for complement-mediated diseases.
Fukuzawa et al. (2017)
15 more