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National Institute of Allergy and Infectious Disease
NIH 3D
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NIH3D

IgG Rabbit Polyclonal Antibody Conjugated to Split Beta-Galactosidase Omega Subunit for Proximity Based Ligation Detection of Analytes

Generated by NIH 3D workflows using data provided by
Rahul Madhu
Created:
3/21/26
Submitted:
3/21/26
Published:
3/21/26
ribbon , colored by secondary structure, not intended for 3D printing
IgG_OmegaFinal-ribbon-secondary-vis_NIH3DRibbon representation colored by secondary structure (a-helix: blue, B-sheet: red, coil: yellow). Not intended for 3D Printing

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surface, colored by by chain, not intended for 3D printingsurface, colored by hydrophobicity, not intended for 3D printingsurface, colored by local charge, not intended for 3D printingsurface, not intended for 3D printingsurface, colored by by chain, print cautionsurface, colored by hydrophobicity, print cautionsurface, colored by local charge, print cautionsurface, print caution
3DPX-023393

Licensing:

CC-BY-ND
How to cite this NIH 3D entry
20
5
Version 1

Category

Biomacromolecules
Biomacromolecules
Description

This 3D model depicts a diagnostic Immunoglobulin G (IgG) antibody conjugated to the Omega subunit of beta-galactosidase (the Enzyme Acceptor).

The omega fragment is a large, inactive polypeptide (approx. 113kDa 997 residues) derived from the LacZ gene. In the ESSENCE platform, this conjugate acts as the primary capture and reporting component. When the target biomarker brings this omega-conjugate into proximity with its complementary alpha-peptide partner, the beta-galactosidase enzyme is reconstituted into its active tetrameric form, facilitating the hydrolysis of colorimetric substrates (e.g., X-gal or CPRG).

Structural Note: Rendered as a high-fidelity surface mesh, this model highlights the significant size of the omega domain relative to the IgG, which is critical for modeling spatial constraints in microfluidic channels.

Source Data Details