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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: Kavitha, M]] | [[Category: Kavitha, M]] | ||
[[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 18:33, 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 MAD1Crystal Structure of the Catalytic Domain of the Inosine Monophosphate Dehydrogenase from Mycobacterium tuberculosis in the complex with IMP and the inhibitor MAD1
Structural highlights
Function[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] |
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