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| - | | + | #REDIRECT [[7mtu]] This PDB entry is obsolete and replaced by 7mtu |
| - | ==Crystal Structure of the Catalytic Domain of the Inosine Monophosphate Dehydrogenase from Bacillus anthracis in the complex with IMP and the inhibitor P221==
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| - | <StructureSection load='5uuw' size='340' side='right'caption='[[5uuw]], [[Resolution|resolution]] 2.34Å' scene=''>
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| - | == Structural highlights ==
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| - | <table><tr><td colspan='2'>[[5uuw]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_cereus_var._anthracis"_(cohn_1872)_smith_et_al._1946 "bacillus cereus var. anthracis" (cohn 1872) smith et al. 1946]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UUW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5UUW FirstGlance]. <br>
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| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=8N1:N-{2-CHLORO-5-[({2-[3-(PROP-1-EN-2-YL)PHENYL]PROPAN-2-YL}CARBAMOYL)AMINO]PHENYL}-BETA-D-XYLOFURANOSYLAMINE'>8N1</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=IMP:INOSINIC+ACID'>IMP</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr>
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| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4myx|4myx]], [[4my8|4my8]], [[4my1|4my1]], [[4mya|4mya]], [[4qm1|4qm1]], [[4my9|4my9]], [[4mjm|4mjm]], [[3tsd|3tsd]], [[3usb|3usb]], [[3tsb|3tsb]], [[5urr|5urr]], [[5urs|5urs]], [[5uuv|5uuv]], [[5uuz|5uuz]]</td></tr>
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| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">guaB, GBAA_0008, A8C77_00065, ABW01_29210 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1392 "Bacillus cereus var. anthracis" (Cohn 1872) Smith et al. 1946])</td></tr>
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| - | <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>
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| - | <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=5uuw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5uuw OCA], [http://pdbe.org/5uuw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5uuw RCSB], [http://www.ebi.ac.uk/pdbsum/5uuw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5uuw ProSAT]</span></td></tr>
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| - | </table>
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| - | == Function ==
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| - | [[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]
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| - | ==See Also==
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| - | *[[Inosine monophosphate dehydrogenase 3D structures|Inosine monophosphate dehydrogenase 3D structures]]
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| - | __TOC__
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| - | </StructureSection>
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| - | [[Category: IMP dehydrogenase]]
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| - | [[Category: Large Structures]]
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| - | [[Category: Anderson, W F]]
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| - | [[Category: Structural genomic]]
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| - | [[Category: Gollapalli, D]]
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| - | [[Category: Gu, M]]
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| - | [[Category: Hedstrom, L]]
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| - | [[Category: Joachimiak, A]]
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| - | [[Category: Kim, Y]]
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| - | [[Category: Makowska-Grzyska, M]]
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| - | [[Category: Maltseva, N]]
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| - | [[Category: Csgid]]
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| - | [[Category: Delta cb]]
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| - | [[Category: Impdh]]
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| - | [[Category: Oxidoreductase]]
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| - | [[Category: Oxidoreductase-oxidoreductase inhibitor complex]]
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| - | [[Category: Tim barrel]]
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