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National Institute of Allergy and Infectious Disease
NIH 3D
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NIH3D

BAX apoptosis regulator

Generated by NIH 3D workflows using data provided by
Jeff Miller
Created:
5/16/25
Submitted:
10/9/26
Published:
10/9/26
BAX apoptosis regulator. thin ribbon, secondary structure
af-q07812-f1-model_v4-ribbon-thin-secondaryBAX apoptosis regulator. Thin ribbon representation colored by secondary structure (a-helix: blue, B-sheet: red, coil: yellow).

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BAX apoptosis regulator. thin ribbon, secondary structureBAX apoptosis regulator. thin ribbon, rainbowBAX apoptosis regulator. thin ribbon, by chainBAX apoptosis regulator. thin ribbon, no colorBAX apoptosis regulator. thick ribbon, secondary structure, print cautionBAX apoptosis regulator. thick ribbon, rainbow, print cautionBAX apoptosis regulator. thick ribbon, by chain, print cautionBAX apoptosis regulator. thick ribbon, no color, NIH 3D repaired

BAX apoptosis regulator. lo-res mol surface, by chainBAX apoptosis regulator. lo-res mol surface, hydrophobicityBAX apoptosis regulator. lo-res mol surface, coulombicBAX apoptosis regulator. lo-res mol surface, no colorBAX apoptosis regulator. hi-res mol surface, by chain, print cautionBAX apoptosis regulator. hi-res mol surface, hydrophobicity, print cautionBAX apoptosis regulator. hi-res mol surface, coulombic, print cautionBAX apoptosis regulator. hi-res mol surface, no color, print caution

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3DPX-021922

Licensing:

Public Domain
How to cite this NIH 3D entry
189
96
Version 2

Category

Biomacromolecules
Biomacromolecules
Description

BAX plays a role in the mitochondrial apoptotic process. Under normal conditions, BAX is largely cytosolic via constant retrotranslocation from mitochondria to the cytosol mediated by BCL2L1/Bcl-xL, which avoids accumulation of toxic BAX levels at the mitochondrial outer membrane (MOM). Under stress conditions, undergoes a conformation change that causes translocation to the mitochondrion membrane, leading to the release of cytochrome c that then triggers apoptosis

Source Data Details