Hi Chandra,

That is an intriguing question. The problem is that even if you would data mine 
this, the data in the PDB would be incredibly skewed to whatever we managed to 
crystalise. And then there is the problem of poorly modeled metal sites. So the 
true answer will be elusive.
Purely anecdotal, I tend to see more monodentate metal binding in protein 
structures. Apart from confirmation bias, it might be caused by bidentate 
coordination almost always having suboptimal geometry in terms of orbital 
overlap. Another issue is that monodentate binding is more evolutionary robust. 
In many metal sites you don’t need direct charge compensation by a formal 
charge. Polarisation is quite enough. That means that your coordinating oxygen 
can be replaced by quite a few residues. This is not the case in a bidentate 
setup.

HTH,
Robbie

From: CCP4 bulletin board [mailto:[email protected]] On Behalf Of Chandra 
Prakash Tiwari
Sent: Monday, July 15, 2019 12:44
To: [email protected]
Subject: [ccp4bb] Bidentate GLU vs two monodentate GLU in metalloproteins

Dear all,
What is more preferable or conserved by evolution point of view between 
glutamate acting as bidentate ligand by its carboxylate group or two 
monodentate GLU at metal binding site in natural metalloprotein.
I was thinking 2 GLU are better than one bidentate GLU because if one GLU gets 
mutated other GLU will still be able to form a coordination bond to a metal.
Please comment and help if i am right or wrong.

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