3r25: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
No edit summary
OCA (talk | contribs)
No edit summary
 
(4 intermediate revisions by the same user not shown)
Line 1: Line 1:
'''Unreleased structure'''


The entry 3r25 is ON HOLD  until Paper Publication
==Crystal structure of enolase superfamily member from Vibrionales bacterium complexed with Mg and Glycerol in the active site==
<StructureSection load='3r25' size='340' side='right'caption='[[3r25]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3r25]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Vibrionales_bacterium_SWAT-3 Vibrionales bacterium SWAT-3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3R25 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3R25 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.603&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3r25 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3r25 OCA], [https://pdbe.org/3r25 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3r25 RCSB], [https://www.ebi.ac.uk/pdbsum/3r25 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3r25 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/IMAND_VIBBS IMAND_VIBBS] Has no detectable activity with D-mannonate and with a panel of 70 other acid sugars (in vitro), in spite of the conservation of the residues that are expected to be important for catalytic activity and cofactor binding. May have evolved a divergent function.<ref>PMID:24697546</ref>


Authors: Fedorov, A.A., Fedorov, E.V., Wichelecki, D., Gerlt, J.A., Almo, S.C.
==See Also==
 
*[[Enolase 3D structures|Enolase 3D structures]]
Description: Crystal structure of enolase superfamily member from VIBRIONALES BACTERIUM complexed with Mg and Glycerol in the active site
*[[Mandelate racemase|Mandelate racemase]]
*[[Mandelate racemase/muconate lactonizing enzyme 3D structures|Mandelate racemase/muconate lactonizing enzyme 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Vibrionales bacterium SWAT-3]]
[[Category: Almo SC]]
[[Category: Fedorov AA]]
[[Category: Fedorov EV]]
[[Category: Gerlt JA]]
[[Category: Wichelecki D]]

Latest revision as of 10:51, 21 February 2024

Crystal structure of enolase superfamily member from Vibrionales bacterium complexed with Mg and Glycerol in the active site

3r25, resolution 1.60Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA