5c6u
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Rv3722c aminotransferase from Mycobacterium tuberculosis== | |
| + | <StructureSection load='5c6u' size='340' side='right'caption='[[5c6u]], [[Resolution|resolution]] 1.83Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5c6u]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_H37Rv Mycobacterium tuberculosis H37Rv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5C6U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5C6U 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]] 1.83Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=5c6u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c6u OCA], [https://pdbe.org/5c6u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5c6u RCSB], [https://www.ebi.ac.uk/pdbsum/5c6u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5c6u ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/ASPAT_MYCTU ASPAT_MYCTU] Main aspartate aminotransferase that couples nitrogen assimilation to aspartate synthesis. Has a weak, but significant, side activity toward kynurenine (Kyn). Oxaloacetate and 2-oxoglutarate, but not pyruvate, serve as amino acceptors, while Asp, Glu and Kyn serve as the best amino donors. Essential for axenic growth and survival of M.tuberculosis in macrophages and in mice.<ref>PMID:32327655</ref> | ||
| - | + | ==See Also== | |
| - | + | *[[Aminotransferase 3D structures|Aminotransferase 3D structures]] | |
| - | + | == References == | |
| - | [[ | + | <references/> |
| - | [[Category: | + | __TOC__ |
| - | [[Category: | + | </StructureSection> |
| - | [[Category: Babnigg | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Mycobacterium tuberculosis H37Rv]] |
| - | [[Category: | + | [[Category: Babnigg G]] |
| - | [[Category: Jedrzejczak | + | [[Category: Hatzos-Skintges C]] |
| - | [[Category: | + | [[Category: JOACHIMIAK A]] |
| + | [[Category: Jedrzejczak R]] | ||
| + | [[Category: OSIPIUK J]] | ||
| + | [[Category: Sacchettini J]] | ||
Current revision
Rv3722c aminotransferase from Mycobacterium tuberculosis
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