› 1zea

X-ray diffraction
1.78Å resolution

Structure of the anti-cholera toxin antibody Fab fragment TE33 in complex with a D-peptide

Released:
DOI: 10.2210/pdb1zea/pdb
PDB entry 1zea coloured by chain, front view.
PDB entry 1zea coloured by chain, side view.
PDB entry 1zea coloured by chain, top view.
Source organisms:
Primary publication:
Structure of an anti-cholera toxin antibody Fab in complex with an epitope-derived D-peptide: a case of polyspecific recognition.
Scheerer P, Kramer A, Otte L, Seifert M, Wessner H, Scholz C, Krauss N, Schneider-Mergener J, Höhne W
J Mol Recognit 20 263-74
PMID: 17712773

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
PDBe Complex ID:
PDB-CPX-106879 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Ig-like domain-containing protein Chain: L
Molecule details ›
Chain: L
Length: 216 amino acids
Theoretical weight: 23.84 KDa
Source organism: Mus musculus
UniProt:
  • Canonical: A2NHM3 (Residues: 1-216; Coverage: 99%)
Gene names: Igk-C, Igkc
Sequence domains:
Structure domains: Immunoglobulins
Ig-like domain-containing protein Chain: H
Molecule details ›
Chain: H
Length: 216 amino acids
Theoretical weight: 23.41 KDa
Source organism: Mus musculus
UniProt:
  • Canonical: Q921A6 (Residues: 1-118; Coverage: 48%)
Sequence domains: Immunoglobulin V-set domain
Structure domains: Immunoglobulins
short synthetic D-amino acid peptide D2 Chain: A
Molecule details ›
Chain: A
Length: 9 amino acids
Theoretical weight: 990 Da
Source organism: synthetic construct
Expression system: Not provided

Ligands and Environments

1 bound ligand:
Ligand CIT 2 x CIT
7 modified residues:
Ligand DVA 1 x DVA
Ligand DPR 1 x DPR
Ligand DSN 2 x DSN
Ligand DGN 1 x DGN
Ligand DHI 1 x DHI
Ligand DTY 1 x DTY
Ligand DAS 1 x DAS

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X13
Spacegroup: P21212
Unit cell:
a: 100.638Å b: 108.862Å c: 40.21Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.201 0.198 0.248
Expression system: Not provided

Quick links

Citations

5 citation in other articles

Linear and extended: a common polyglutamine conformation recognized by the three antibodies MW1, 1C2 and 3B5H10.
Klein et al. (2013)
4 more

3 mentions without citation

Structural evidence for a bifurcated mode of action in the antibody-mediated neutralization of hepatitis C virus.
Deng et al. (2013)
2 more