6mgu: Difference between revisions
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==Crystal Structure of the Catalytic Domain of the Inosine Monophosphate Dehydrogenase from Bacillus Anthracis in the complex with inhibitor Oxanosine monophosphate== | |||
<StructureSection load='6mgu' size='340' side='right' caption='[[6mgu]], [[Resolution|resolution]] 1.54Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6mgu]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MGU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6MGU FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=JQS:5-[(Z)-(aminomethylidene)amino]-1-(5-O-phosphono-beta-D-ribofuranosyl)-1H-imidazole-4-carboxylic+acid'>JQS</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene></td></tr> | |||
[[Category: | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/IMP_dehydrogenase IMP dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.205 1.1.1.205] </span></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=6mgu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mgu OCA], [http://pdbe.org/6mgu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6mgu RCSB], [http://www.ebi.ac.uk/pdbsum/6mgu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6mgu ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/A0A0J1HJU0_BACAN A0A0J1HJU0_BACAN]] 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: IMP dehydrogenase]] | |||
[[Category: Structural genomic]] | |||
[[Category: Hedstrom, L]] | |||
[[Category: Joachimiak, A]] | |||
[[Category: Kim, Y]] | |||
[[Category: Maltseva, N]] | |||
[[Category: Yu, R]] | [[Category: Yu, R]] | ||
[[Category: | [[Category: Csgid]] | ||
[[Category: | [[Category: Delta cb]] | ||
[[Category: | [[Category: Impdh]] | ||
[[Category: | [[Category: Oxidoreductase]] | ||
[[Category: | [[Category: Oxidoreductase-oxidoreductase inhibitor complex]] | ||
[[Category: Tim barrel]] | |||
Revision as of 06:06, 24 October 2018
Crystal Structure of the Catalytic Domain of the Inosine Monophosphate Dehydrogenase from Bacillus Anthracis in the complex with inhibitor Oxanosine monophosphate
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