This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
5drc
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
==Crystal structure of Mycobacterium tuberculosis malate synthase in complex with 2-hydroxy-4-(1H-indol-3-yl)-4-oxobut-2-enoic acid== | ==Crystal structure of Mycobacterium tuberculosis malate synthase in complex with 2-hydroxy-4-(1H-indol-3-yl)-4-oxobut-2-enoic acid== | ||
| - | <StructureSection load='5drc' size='340' side='right' caption='[[5drc]], [[Resolution|resolution]] 2.18Å' scene=''> | + | <StructureSection load='5drc' size='340' side='right'caption='[[5drc]], [[Resolution|resolution]] 2.18Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5drc]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[5drc]] 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=5DRC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5DRC FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.18Å</td></tr> |
| - | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5ER:(2Z)-2-HYDROXY-4-(1H-INDOL-3-YL)-4-OXOBUT-2-ENOIC+ACID'>5ER</scene>, <scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</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=5drc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5drc OCA], [https://pdbe.org/5drc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5drc RCSB], [https://www.ebi.ac.uk/pdbsum/5drc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5drc ProSAT]</span></td></tr> | |
| - | + | ||
| - | + | ||
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/MASZ_MYCTU MASZ_MYCTU] Involved in the glycolate utilization. Catalyzes the condensation and subsequent hydrolysis of acetyl-coenzyme A (acetyl-CoA) and glyoxylate to form malate and CoA (By similarity).[HAMAP-Rule:MF_00641] |
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 22: | Line 19: | ||
</div> | </div> | ||
<div class="pdbe-citations 5drc" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 5drc" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Malate synthase 3D structures|Malate synthase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Mycobacterium tuberculosis H37Rv]] |
| - | [[Category: Huang | + | [[Category: Huang H-L]] |
| - | [[Category: Sacchettini | + | [[Category: Sacchettini JC]] |
| - | + | ||
| - | + | ||
Current revision
Crystal structure of Mycobacterium tuberculosis malate synthase in complex with 2-hydroxy-4-(1H-indol-3-yl)-4-oxobut-2-enoic acid
| |||||||||||
