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National Institute of Allergy and Infectious Disease
NIH 3D
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NIH3D

CRYSTAL STRUCTURE OF BOVINE BETA-ARRESTIN 1

Generated by NIH 3D workflows using data provided by
kozar@stanford.edu
Created:
8/8/23
Submitted:
10/9/26
Published:
10/9/26
1G4M Single Chain. thin ribbon, secondary structure
1g4m_edited-ribbon-thin-secondary1G4M Single Chain. Thin ribbon representation colored by secondary structure (a-helix: blue, B-sheet: red, coil: yellow).

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1G4M Single Chain. thin ribbon, secondary structure1G4M Single Chain. thin ribbon, rainbow1G4M Single Chain. thin ribbon, by chain1G4M Single Chain. thin ribbon, no color1G4M Single Chain. thick ribbon, secondary structure, print caution1G4M Single Chain. thick ribbon, rainbow, print caution1G4M Single Chain. thick ribbon, by chain, print caution1G4M Single Chain. thick ribbon, no color, NIH 3D repaired

1G4M Single Chain. lo-res mol surface, by chain1G4M Single Chain. lo-res mol surface, hydrophobicity1G4M Single Chain. lo-res mol surface, coulombic1G4M Single Chain. lo-res mol surface, no color1G4M Single Chain. hi-res mol surface, by chain, print caution1G4M Single Chain. hi-res mol surface, hydrophobicity, print caution1G4M Single Chain. hi-res mol surface, coulombic, print caution1G4M Single Chain. hi-res mol surface, no color, print caution

Learn more about NIH 3D workflow outputs

3DPX-020347

Licensing:

Public Domain
How to cite this NIH 3D entry
145
51
Version 2

Category

Biomacromolecules
Biomacromolecules
Description

Single chain A.

Arrestins are responsible for the desensitization of many sequence-divergent G protein-coupled receptors. They compete with G proteins for binding to activated phosphorylated receptors, initiate receptor internalization, and activate additional signaling pathways

Source Data Details
3D Printing Instructions