› 8ftg

X-ray diffraction
1.13Å resolution

Biophysical and Structural Characterization of an Anti-Caffeine VHH Antibody

Released:
DOI: 10.2210/pdb8ftg/pdb
Model geometry
Fit model/data
PDB entry 8ftg coloured by chain, front view.
PDB entry 8ftg coloured by chain, side view.
PDB entry 8ftg coloured by chain, top view.
Source organism: Lama glama
Primary publication:
Molecular recognition requires dimerization of a VHH antibody.
Smith CA, Sonneson GJ, Hoey RJ, Hinerman JM, Sheehy K, Walter R, Herr AB, Horn JR
OpenAccess logo MAbs 15 2215363 (2023)
PMID: 37243579

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-226532 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Anti-Caffeine VHH Antibody Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 121 amino acids
Theoretical weight: 13.17 KDa
Source organism: Lama glama
Expression system: Escherichia coli

Ligands and Environments

3 bound ligands:
Ligand CFF 4 x CFF
Ligand TRS 1 x TRS
Ligand CL 3 x CL
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: APS BEAMLINE 22-BM
Spacegroup: P1
Unit cell:
a: 50.136Å b: 66.28Å c: 68.999Å
α: 111.62° β: 95.2° γ: 90.25°
R-values:
R R work R free
0.144 0.142 0.164
Expression system: Escherichia coli

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Citations

1 mention without citation

Molecular recognition requires dimerization of a VHH antibody.
Smith et al. (2023)