6nbm
From Proteopedia
(Difference between revisions)
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==CRYSTAL STRUCTURE OF ENOLASE FROM LEGIONELLA PNEUMOPHILA BOUND TO PHOSPHATE AND MAGNESIUM== | ==CRYSTAL STRUCTURE OF ENOLASE FROM LEGIONELLA PNEUMOPHILA BOUND TO PHOSPHATE AND MAGNESIUM== | ||
| - | <StructureSection load='6nbm' size='340' side='right' caption='[[6nbm]], [[Resolution|resolution]] 1.90Å' scene=''> | + | <StructureSection load='6nbm' size='340' side='right'caption='[[6nbm]], [[Resolution|resolution]] 1.90Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6nbm]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6NBM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6NBM FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6nbm]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_33152 Atcc 33152]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6NBM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6NBM FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6nb2|6nb2]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6nb2|6nb2]]</td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">eno, C3927_09475 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=446 ATCC 33152])</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphopyruvate_hydratase Phosphopyruvate hydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.11 4.2.1.11] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphopyruvate_hydratase Phosphopyruvate hydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.11 4.2.1.11] </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=6nbm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6nbm OCA], [http://pdbe.org/6nbm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6nbm RCSB], [http://www.ebi.ac.uk/pdbsum/6nbm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6nbm ProSAT]</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=6nbm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6nbm OCA], [http://pdbe.org/6nbm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6nbm RCSB], [http://www.ebi.ac.uk/pdbsum/6nbm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6nbm ProSAT]</span></td></tr> | ||
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== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/A0A2S6F4U1_LEGPN A0A2S6F4U1_LEGPN]] Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis.[HAMAP-Rule:MF_00318] | [[http://www.uniprot.org/uniprot/A0A2S6F4U1_LEGPN A0A2S6F4U1_LEGPN]] Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis.[HAMAP-Rule:MF_00318] | ||
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| + | ==See Also== | ||
| + | *[[Enolase 3D structures|Enolase 3D structures]] | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Atcc 33152]] | ||
| + | [[Category: Large Structures]] | ||
[[Category: Phosphopyruvate hydratase]] | [[Category: Phosphopyruvate hydratase]] | ||
[[Category: Structural genomic]] | [[Category: Structural genomic]] | ||
[[Category: Lyase]] | [[Category: Lyase]] | ||
[[Category: Ssgcid]] | [[Category: Ssgcid]] | ||
Revision as of 11:24, 18 December 2019
CRYSTAL STRUCTURE OF ENOLASE FROM LEGIONELLA PNEUMOPHILA BOUND TO PHOSPHATE AND MAGNESIUM
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