4hnl
From Proteopedia
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==Crystal structure of ENOLASE EGBG_01401 (TARGET EFI-502226) from Enterococcus gallinarum EG2== | ==Crystal structure of ENOLASE EGBG_01401 (TARGET EFI-502226) from Enterococcus gallinarum EG2== | ||
<StructureSection load='4hnl' size='340' side='right' caption='[[4hnl]], [[Resolution|resolution]] 1.48Å' scene=''> | <StructureSection load='4hnl' size='340' side='right' caption='[[4hnl]], [[Resolution|resolution]] 1.48Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[4hnl]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[4hnl]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Enterococcus_gallinarum_1,134,897 Enterococcus gallinarum 1,134,897]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HNL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4HNL 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=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=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">EGBG_01401 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=565653 Enterococcus gallinarum | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">EGBG_01401 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=565653 Enterococcus gallinarum 1,134,897])</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=4hnl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hnl OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4hnl RCSB], [http://www.ebi.ac.uk/pdbsum/4hnl 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=4hnl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hnl OCA], [http://pdbe.org/4hnl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4hnl RCSB], [http://www.ebi.ac.uk/pdbsum/4hnl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4hnl ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [[http://www.uniprot.org/uniprot/ | + | [[http://www.uniprot.org/uniprot/IMND1_ENTGA IMND1_ENTGA]] Has no detectable activity with D-mannonate and with a panel of 70 other acid sugars (in vitro), in spite of the conservation of the residues that are expected to be important for catalytic activity and cofactor binding. May have evolved a divergent function.<ref>PMID:24697546</ref> |
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Enterococcus gallinarum | + | [[Category: Enterococcus gallinarum 1,134,897]] |
[[Category: Almo, S C]] | [[Category: Almo, S C]] | ||
[[Category: Bhosle, R]] | [[Category: Bhosle, R]] | ||
Revision as of 13:14, 11 August 2016
Crystal structure of ENOLASE EGBG_01401 (TARGET EFI-502226) from Enterococcus gallinarum EG2
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Categories: Enterococcus gallinarum 1,134,897 | 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 | Love, J | Obaidi, N F.Al | Patskovsky, Y | Seidel, R D | Stead, M | Toro, R | Washington, E | Zencheck, W D | Dehydratase | Enzyme function initiative | Isomerase | Magnesium binding
