3onf: Difference between revisions

No edit summary
No edit summary
 
(2 intermediate revisions by the same user not shown)
Line 1: Line 1:
==Crystal structure of Lupinus luteus S-adenosyl-L-homocysteine hydrolase in complex with cordycepin==
==Crystal structure of Lupinus luteus S-adenosyl-L-homocysteine hydrolase in complex with cordycepin==
<StructureSection load='3onf' size='340' side='right' caption='[[3onf]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='3onf' size='340' side='right'caption='[[3onf]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3onf]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/European_yellow_lupin European yellow lupin]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ONF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ONF FirstGlance]. <br>
<table><tr><td colspan='2'>[[3onf]] 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=3ONF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ONF FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=3AD:3-DEOXYADENOSINE'>3AD</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>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1a7a|1a7a]], [[1b3r|1b3r]], [[1v8b|1v8b]], [[3ce6|3ce6]], [[3ond|3ond]], [[3one|3one]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3AD:3-DEOXYADENOSINE'>3AD</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>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SAHH, SHH, ssh-1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3873 European yellow lupin])</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=3onf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3onf OCA], [https://pdbe.org/3onf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3onf RCSB], [https://www.ebi.ac.uk/pdbsum/3onf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3onf ProSAT]</span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Adenosylhomocysteinase Adenosylhomocysteinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.3.1.1 3.3.1.1] </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=3onf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3onf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3onf RCSB], [http://www.ebi.ac.uk/pdbsum/3onf PDBsum]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://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).  
[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 ==
Line 19: Line 18:
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
<div class="pdbe-citations 3onf" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
Line 26: Line 26:
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Adenosylhomocysteinase]]
[[Category: Large Structures]]
[[Category: European yellow lupin]]
[[Category: Lupinus luteus]]
[[Category: Brzezinski, K]]
[[Category: Brzezinski K]]
[[Category: Jaskolski, M]]
[[Category: Jaskolski M]]
[[Category: Enzyme-inhibitor complex]]
[[Category: Hydrolase-hydrolase inhibitor complex]]
[[Category: Nad cofactor]]
[[Category: Plant protein]]
[[Category: Regulation of sam-dependent methylation reaction]]

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA