Dear Christian,

Kleywegt (1996; "Use of Non-crystallographic Symmetry in Protein
Structure Refinement." Acta Cryst D52, 842-857. DOI:
10.1107/S0907444995016477) reported that NCS-related molecules tend to
be similar but differences in ligand binding do sometimes occur (cited
Sevcik et al. 1996 in that paper).

We saw a similar difference (coenzyme absent/present; co-crystallized)
between 2 biologically monomeric NCS-related protein molecules
apparently due to crystal contact differences (Sidhu et al. 2011;
"Structure of a highly NADP+-specific isocitrate dehydrogenase." Acta
Cryst. D67, 856-869. DOI: 10.1107/S0907444911028575).

Best wishes,
Navdeep


---
On 27.10.20 11:19, Christian GALICIA wrote:
> Hello,
> In our structure only one chain in a crystallographic trimer
> (non-biological) shows a ligand bound to it (with clear density). There
> doesn't seem to be any channels (or lack of them) favoring that specific
> site. Can the community give your opinion on whether this can make the
> presence of the ligand or its biological role questionable, and give any
> examples of similar cases you might be aware of. Thank you.
> -- 
> *Christian Galicia*
> Post Doctoral Scientist
> E-mail: cgali...@vub.be <mailto:cgali...@vub.be>
> 
>  
> 
> 
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