4gme
From Proteopedia
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==Crystal structure of mannonate dehydratase (target EFI-502209) from caulobacter crescentus cb15 complexed with magnesium and d-mannonate== | ==Crystal structure of mannonate dehydratase (target EFI-502209) from caulobacter crescentus cb15 complexed with magnesium and d-mannonate== | ||
<StructureSection load='4gme' size='340' side='right' caption='[[4gme]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='4gme' size='340' side='right' caption='[[4gme]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[4gme]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[4gme]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Caucr Caucr]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GME OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4GME FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CO3:CARBONATE+ION'>CO3</scene>, <scene name='pdbligand=CS2:D-MANNONIC+ACID'>CS2</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CO3:CARBONATE+ION'>CO3</scene>, <scene name='pdbligand=CS2:D-MANNONIC+ACID'>CS2</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | ||
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CC_0532 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id= | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CC_0532 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=190650 CAUCR])</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=4gme FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gme OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4gme RCSB], [http://www.ebi.ac.uk/pdbsum/4gme 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=4gme FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gme OCA], [http://pdbe.org/4gme PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4gme RCSB], [http://www.ebi.ac.uk/pdbsum/4gme PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4gme ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [[http://www.uniprot.org/uniprot/ | + | [[http://www.uniprot.org/uniprot/MAND2_CAUCR MAND2_CAUCR]] Catalyzes the dehydration of D-mannonate. Has no detectable activity with a panel of 70 other acid sugars (in vitro).<ref>PMID:24697546</ref> |
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Caucr]] |
[[Category: Almo, S C]] | [[Category: Almo, S C]] | ||
[[Category: Bhosle, R]] | [[Category: Bhosle, R]] | ||
Revision as of 14:09, 11 August 2016
Crystal structure of mannonate dehydratase (target EFI-502209) from caulobacter crescentus cb15 complexed with magnesium and d-mannonate
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Categories: Caucr | Almo, S C | Bhosle, R | Chowdhury, S | EFI, Enzyme Function Initiative | Evans, B | Gerlt, J A | Glenn, A Scott | Hammonds, J | Hillerich, B | Imker, H J | Patskovsky, Y | Seidel, R D | Toro, R | Washington, E | Zencheck, W D | Efi | Enolase | Enzyme function initiative | Lyase | Magnesium binding site
