Hi

I think the fastest solution to your problem might be restricting the region of 
the complete protein structure from AlphaFold you use for the alignment.
Perhaps selecting just your domain of interest, or maybe a slightly wider 
region maybe including a linker will do the trick.

I suspect the structure of this BH3 domain might be so simple (Is it just a 
single alpha-helix?) that it's to easy for structural alignment software to 
find that motif in other parts of the protein.

How to do this and whether it's an appropriate approach depends on what 
software you're using and what question you're trying to answer

Hope this helps
Aderik
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From: CCP4 bulletin board <[email protected]> on behalf of Thripthi Shenoy 
<[email protected]>
Sent: Wednesday, February 11, 2026 5:27 AM
To: [email protected] <[email protected]>
Subject: [ccp4bb] Query regarding the structure-based sequence alignment


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Greetings to all,

I am currently working on understanding the structure-based sequence alignment 
of the crystal structure of NOXA BH3 domain and the complete protein structure 
obtained from AlphaFold. According to my understanding, the BH3 binding domain 
from the crystal structure should get aligned with the BH3 domain in the entire 
protein structure. However, this is not the case and the identical amino acids 
of the BH3 domains are not getting aligned. I would be grateful to know if this 
is a correct approach to proceed with the structure based protein alignment.

Thanking you in advance
With regards,
Thripthi S.

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