4pgf: Difference between revisions

Line 1:

'''~~Unreleased structure~~'''

==The structure of mono-acetylated SAHH==

~~The entry~~ 4pgf is ~~ON HOLD until Paper Publication~~

== Structural highlights ==

<table><tr><td colspan='2'>[[4pgf]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PGF OCA]. For a guided tour on the structure components use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PGF FirstGlance].

~~Authors~~: ~~Kavran~~, J.M., ~~Wang~~, Y., Cole, P.A., Leahy, D.J.

</td></tr><tr><td class="sblockLbl">[[Ligand|Ligands:]]</td><td class="sblockDat"><scene name='pdbligand=ADN:ADENOSINE'>ADN</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>

<tr><td class="sblockLbl">[[Non-Standard_Residue|NonStd Res:]]</td><td class="sblockDat"><scene name='pdbligand=ALY:N(6)-ACETYLLYSINE'>ALY</scene></td></tr>

~~Description~~:

<tr><td class="sblockLbl">[[Related_structure|Related:]]</td><td class="sblockDat">[[4pfj|4pfj]]</td></tr>

<tr><td class="sblockLbl">Activity:</td><td class="sblockDat">[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] </td></tr>

<tr><td class="sblockLbl">Resources:</td><td class="sblockDat">[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4pgf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pgf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4pgf RCSB], [http://www.ebi.ac.uk/pdbsum/4pgf PDBsum]</td></tr>

<table>

== Disease ==

[[http://www.uniprot.org/uniprot/SAHH_HUMAN SAHH_HUMAN]] Defects in AHCY are the cause of hypermethioninemia with S-adenosylhomocysteine hydrolase deficiency (HMAHCHD) [MIM:[http://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 ==

[[http://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>

== References ==

__TOC__

</StructureSection>

[[Category: Adenosylhomocysteinase]]

[[Category: Cole, P A.]]

[[Category: Kavran, J M.]]

[[Category: Leahy, D J.]]

[[Category: Wang, Y.]]

[[Category: Hydrolase]]

[[Category: Hydrolyase acetylation sahh semi-synthetic]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
+==The structure of mono-acetylated SAHH==
+<StructureSection load='4pgf' size='340' side='right' caption='[[4pgf]], [[Resolution|resolution]] 2.59&Aring;' scene=''>
-The entry 4pgf is ON HOLD  until Paper Publication
+== Structural highlights ==
+<table><tr><td colspan='2'>[[4pgf]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PGF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PGF FirstGlance]. <br>
-Authors: Kavran, J.M., Wang, Y., Cole, P.A., Leahy, D.J.
+</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADN:ADENOSINE'>ADN</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene><br>
+<tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ALY:N(6)-ACETYLLYSINE'>ALY</scene></td></tr>
-Description:
+<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4pfj|4pfj]]</td></tr>
+<tr><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><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4pgf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pgf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4pgf RCSB], [http://www.ebi.ac.uk/pdbsum/4pgf PDBsum]</span></td></tr>
+<table>
+== Disease ==
+[[http://www.uniprot.org/uniprot/SAHH_HUMAN SAHH_HUMAN]] Defects in AHCY are the cause of hypermethioninemia with S-adenosylhomocysteine hydrolase deficiency (HMAHCHD) [MIM:[http://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 ==
+[[http://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>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Adenosylhomocysteinase]]
+[[Category: Cole, P A.]]
+[[Category: Kavran, J M.]]
+[[Category: Leahy, D J.]]
+[[Category: Wang, Y.]]
+[[Category: Hydrolase]]
+[[Category: Hydrolyase acetylation sahh semi-synthetic]]