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3ond

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Current revision (09:42, 6 September 2023) (edit) (undo)
 
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<StructureSection load='3ond' size='340' side='right'caption='[[3ond]], [[Resolution|resolution]] 1.17&Aring;' scene=''>
<StructureSection load='3ond' size='340' side='right'caption='[[3ond]], [[Resolution|resolution]] 1.17&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3ond]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/European_yellow_lupine European yellow lupine]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OND OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OND FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3ond]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Lupinus_luteus Lupinus luteus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OND OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OND FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADN:ADENOSINE'>ADN</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.17&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1a7a|1a7a]], [[1b3r|1b3r]], [[1v8b|1v8b]], [[3ce6|3ce6]], [[3one|3one]], [[3onf|3onf]]</div></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADN:ADENOSINE'>ADN</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SAHH, SHH, shh-1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3873 European yellow lupine])</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Adenosylhomocysteinase Adenosylhomocysteinase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.3.1.1 3.3.1.1] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3ond FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ond OCA], [https://pdbe.org/3ond PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ond RCSB], [https://www.ebi.ac.uk/pdbsum/3ond PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ond ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3ond FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ond OCA], [https://pdbe.org/3ond PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ond RCSB], [https://www.ebi.ac.uk/pdbsum/3ond PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ond ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/SAHH_LUPLU SAHH_LUPLU]] Adenosylhomocysteine is a competitive inhibitor of S-adenosyl-L-methionine-dependent methyl transferase reactions; therefore adenosylhomocysteinase may play a key role in the control of methylations via regulation of the intracellular concentration of adenosylhomocysteine (By similarity).
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[https://www.uniprot.org/uniprot/SAHH_LUPLU SAHH_LUPLU] Adenosylhomocysteine is a competitive inhibitor of S-adenosyl-L-methionine-dependent methyl transferase reactions; therefore adenosylhomocysteinase may play a key role in the control of methylations via regulation of the intracellular concentration of adenosylhomocysteine (By similarity).
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Adenosylhomocysteinase]]
 
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[[Category: European yellow lupine]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Brzezinski, K]]
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[[Category: Lupinus luteus]]
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[[Category: Jaskolski, M]]
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[[Category: Brzezinski K]]
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[[Category: Enzyme-substrate complex]]
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[[Category: Jaskolski M]]
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[[Category: Nad cofactor]]
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[[Category: Plant protein]]
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[[Category: Regulation of sam-dependent methylation reaction]]
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Current revision

Crystal structure of Lupinus luteus S-adenosyl-L-homocysteine hydrolase in complex with adenosine

PDB ID 3ond

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