4zqp
From Proteopedia
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| - | ''' | + | ==Crystal Structure of the Catalytic Domain of the Inosine Monophosphate Dehydrogenase from Mycobacterium tuberculosis in the complex with IMP and the inhibitor MAD1== |
| - | + | <StructureSection load='4zqp' size='340' side='right' caption='[[4zqp]], [[Resolution|resolution]] 1.90Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[4zqp]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZQP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ZQP FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=IMP:INOSINIC+ACID'>IMP</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=KP3:5-O-({1-[(2E)-4-(4-HYDROXY-6-METHOXY-7-METHYL-3-OXO-1,3-DIHYDRO-2-BENZOFURAN-5-YL)-2-METHYLBUT-2-EN-1-YL]-1H-1,2,3-TRIAZOL-4-YL}METHYL)ADENOSINE'>KP3</scene>, <scene name='pdbligand=PGO:S-1,2-PROPANEDIOL'>PGO</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | |
| - | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4zqm|4zqm]], [[4zqn|4zqn]], [[4zqo|4zqo]]</td></tr> | |
| - | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4zqp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zqp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4zqp RCSB], [http://www.ebi.ac.uk/pdbsum/4zqp PDBsum]</span></td></tr> | |
| - | [[Category: | + | </table> |
| - | [[Category: | + | == Function == |
| + | [[http://www.uniprot.org/uniprot/IMDH_MYCTU IMDH_MYCTU]] Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth.[HAMAP-Rule:MF_01964] | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Andesrson, W F]] | ||
| + | [[Category: Structural genomic]] | ||
| + | [[Category: Gu, M]] | ||
| + | [[Category: Hedstrom, L]] | ||
[[Category: Joachimiak, A]] | [[Category: Joachimiak, A]] | ||
| - | [[Category: Makowska-Grzyska, M]] | ||
[[Category: Kavitha, M]] | [[Category: Kavitha, M]] | ||
| - | [[Category: Hedstrom, L]] | ||
| - | [[Category: Gu, M]] | ||
| - | [[Category: Center For Structural Genomics Of Infectious Diseases (Csgid)]] | ||
[[Category: Kim, Y]] | [[Category: Kim, Y]] | ||
| + | [[Category: Makowska-Grzyska, M]] | ||
| + | [[Category: Center for membrane proteins of infectious disease]] | ||
| + | [[Category: Delta cb]] | ||
| + | [[Category: Impdh]] | ||
| + | [[Category: Mad1]] | ||
Revision as of 15:33, 17 June 2015
Crystal Structure of the Catalytic Domain of the Inosine Monophosphate Dehydrogenase from Mycobacterium tuberculosis in the complex with IMP and the inhibitor MAD1
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