4myx: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4myx]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MYX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4MYX FirstGlance]. <br> | <table><tr><td colspan='2'>[[4myx]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MYX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4MYX FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=2F0:2-CHLORO-5-{[(2-{3-[(1E)-N-HYDROXYETHANIMIDOYL]PHENYL}PROPAN-2-YL)CARBAMOYL]AMINO}BENZAMIDE'>2F0</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=IMP:INOSINIC+ACID'>IMP</scene>, <scene name='pdbligand=MLI:MALONATE+ION'>MLI</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>< | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=2F0:2-CHLORO-5-{[(2-{3-[(1E)-N-HYDROXYETHANIMIDOYL]PHENYL}PROPAN-2-YL)CARBAMOYL]AMINO}BENZAMIDE'>2F0</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=IMP:INOSINIC+ACID'>IMP</scene>, <scene name='pdbligand=MLI:MALONATE+ION'>MLI</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3tsb|3tsb]], [[3tsd|3tsd]], [[3usb|3usb]], [[4mjm|4mjm]], [[4mxs|4mxs]], [[4my1|4my1]], [[4my8|4my8]], [[4my9|4my9]], [[4mya|4mya]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3tsb|3tsb]], [[3tsd|3tsd]], [[3usb|3usb]], [[4mjm|4mjm]], [[4mxs|4mxs]], [[4my1|4my1]], [[4my8|4my8]], [[4my9|4my9]], [[4mya|4mya]]</td></tr> | ||
<tr><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='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><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4myx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4myx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4myx RCSB], [http://www.ebi.ac.uk/pdbsum/4myx PDBsum]</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=4myx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4myx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4myx RCSB], [http://www.ebi.ac.uk/pdbsum/4myx PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/Q81W29_BACAN Q81W29_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 (By similarity).[HAMAP-Rule:MF_01964] | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: IMP dehydrogenase]] | [[Category: IMP dehydrogenase]] | ||
[[Category: Anderson, W F | [[Category: Anderson, W F]] | ||
[[Category: | [[Category: Structural genomic]] | ||
[[Category: Csgid]] | [[Category: Csgid]] | ||
[[Category: Gu, M | [[Category: Gu, M]] | ||
[[Category: Joachimiak, A | [[Category: Joachimiak, A]] | ||
[[Category: Kim, Y | [[Category: Kim, Y]] | ||
[[Category: Makowska-Grzyska, M | [[Category: Makowska-Grzyska, M]] | ||
[[Category: Alpha-beta structure]] | [[Category: Alpha-beta structure]] | ||
[[Category: National institute of allergy and infectious disease]] | [[Category: National institute of allergy and infectious disease]] | ||
[[Category: Niaid]] | [[Category: Niaid]] | ||
[[Category: Oxidoreductase-oxidoreductase inhibitor complex]] | [[Category: Oxidoreductase-oxidoreductase inhibitor complex]] | ||
[[Category: Tim barrel]] | [[Category: Tim barrel]] | ||
Revision as of 09:37, 25 December 2014
Crystal Structure of the Inosine 5'-monophosphate Dehydrogenase, with a Internal Deletion of CBS Domain from Bacillus anthracis str. Ame complexed with P32Crystal Structure of the Inosine 5'-monophosphate Dehydrogenase, with a Internal Deletion of CBS Domain from Bacillus anthracis str. Ame complexed with P32
Structural highlights
Function[Q81W29_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 (By similarity).[HAMAP-Rule:MF_01964] |
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