This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
3nj4
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
==Fluoro-neplanocin A in Human S-Adenosylhomocysteine Hydrolase== | ==Fluoro-neplanocin A in Human S-Adenosylhomocysteine Hydrolase== | ||
| - | <StructureSection load='3nj4' size='340' side='right' caption='[[3nj4]], [[Resolution|resolution]] 2.50Å' scene=''> | + | <StructureSection load='3nj4' size='340' side='right'caption='[[3nj4]], [[Resolution|resolution]] 2.50Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3nj4]] is a 4 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[3nj4]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NJ4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NJ4 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AFX:(4S,5S)-4-(6-AMINO-9H-PURIN-9-YL)-3-FLUORO-5-HYDROXY-2-(HYDROXYMETHYL)CYCLOPENT-2-EN-1-ONE'>AFX</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AFX:(4S,5S)-4-(6-AMINO-9H-PURIN-9-YL)-3-FLUORO-5-HYDROXY-2-(HYDROXYMETHYL)CYCLOPENT-2-EN-1-ONE'>AFX</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AHCY, SAHH ([ | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AHCY, SAHH ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <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> |
| - | <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=3nj4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nj4 OCA], [https://pdbe.org/3nj4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3nj4 RCSB], [https://www.ebi.ac.uk/pdbsum/3nj4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3nj4 ProSAT]</span></td></tr> |
</table> | </table> | ||
== Disease == | == Disease == | ||
| - | [[ | + | [[https://www.uniprot.org/uniprot/SAHH_HUMAN SAHH_HUMAN]] Defects in AHCY are the cause of hypermethioninemia with S-adenosylhomocysteine hydrolase deficiency (HMAHCHD) [MIM:[https://omim.org/entry/613752 613752]]. A metabolic disorder characterized by hypermethioninemia associated with failure to thrive, mental and motor retardation, facial dysmorphism with abnormal hair and teeth, and myocardiopathy.<ref>PMID:15024124</ref> <ref>PMID:16736098</ref> <ref>PMID:19177456</ref> <ref>PMID:20852937</ref> |
== Function == | == Function == | ||
| - | [[ | + | [[https://www.uniprot.org/uniprot/SAHH_HUMAN SAHH_HUMAN]] 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.<ref>PMID:12590576</ref> |
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 31: | Line 31: | ||
[[Category: Adenosylhomocysteinase]] | [[Category: Adenosylhomocysteinase]] | ||
[[Category: Human]] | [[Category: Human]] | ||
| + | [[Category: Large Structures]] | ||
[[Category: Choi, S]] | [[Category: Choi, S]] | ||
[[Category: Heo, Y S]] | [[Category: Heo, Y S]] | ||
Revision as of 07:03, 12 May 2022
Fluoro-neplanocin A in Human S-Adenosylhomocysteine Hydrolase
| |||||||||||
