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3v4b
From Proteopedia
(Difference between revisions)
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==Crystal structure of an enolase from the soil bacterium Cellvibrio japonicus (TARGET EFI-502161) with bound MG and L-tartrate== | ==Crystal structure of an enolase from the soil bacterium Cellvibrio japonicus (TARGET EFI-502161) with bound MG and L-tartrate== | ||
| - | <StructureSection load='3v4b' size='340' side='right' caption='[[3v4b]], [[Resolution|resolution]] 1.40Å' scene=''> | + | <StructureSection load='3v4b' size='340' side='right'caption='[[3v4b]], [[Resolution|resolution]] 1.40Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3v4b]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[3v4b]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Celju Celju]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3V4B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3V4B 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=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3v3w|3v3w]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3v3w|3v3w]]</div></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">rspA, CJA_3069 ([ | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">rspA, CJA_3069 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=498211 CELJU])</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3v4b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3v4b OCA], [https://pdbe.org/3v4b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3v4b RCSB], [https://www.ebi.ac.uk/pdbsum/3v4b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3v4b ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [[ | + | [[https://www.uniprot.org/uniprot/MAND_CELJU MAND_CELJU]] Has low D-mannonate dehydratase activity (in vitro), suggesting that this is not a physiological substrate and that it has no significant role in D-mannonate degradation in vivo. Has no detectable activity with a panel of 70 other acid sugars (in vitro).<ref>PMID:24697546</ref> |
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Celju]] | [[Category: Celju]] | ||
| + | [[Category: Large Structures]] | ||
[[Category: Almo, S C]] | [[Category: Almo, S C]] | ||
[[Category: Bhosle, R]] | [[Category: Bhosle, R]] | ||
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[[Category: Enzyme function initiative]] | [[Category: Enzyme function initiative]] | ||
[[Category: Lyase]] | [[Category: Lyase]] | ||
| + | [[Category: Structural genomic]] | ||
Revision as of 08:29, 20 July 2022
Crystal structure of an enolase from the soil bacterium Cellvibrio japonicus (TARGET EFI-502161) with bound MG and L-tartrate
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Categories: Celju | Large Structures | 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 | Morisco, L L | Obaidi, N Al | Seidel, R D | Sojitra, S | Toro, R | Vetting, M W | Washington, E | Wasserman, S R | Zencheck, W D | Efi | Enolase | Enzyme function initiative | Lyase | Structural genomic
