4yvf

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'''Unreleased structure'''
 
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The entry 4yvf is ON HOLD until Paper Publication
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==Structure of S-adenosyl-L-homocysteine hydrolase==
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<StructureSection load='4yvf' size='340' side='right'caption='[[4yvf]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
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Authors: Akiko, K.
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4yvf]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YVF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4YVF FirstGlance]. <br>
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Description: Structure of S-adenosyl-L-homocysteine hydrolase
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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]] 2.7&#8491;</td></tr>
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[[Category: Unreleased Structures]]
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAI:1,4-DIHYDRONICOTINAMIDE+ADENINE+DINUCLEOTIDE'>NAI</scene>, <scene name='pdbligand=XFA:2-{[5-CHLORO-2-(4-CHLOROPHENOXY)PHENYL](2-{[2-(METHYLAMINO)ETHYL]AMINO}-2-OXOETHYL)AMINO}-N-(1,3-DIHYDRO-2H-ISOINDOL-2-YL)-N-METHYLACETAMIDE'>XFA</scene></td></tr>
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[[Category: Akiko, K]]
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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=4yvf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yvf OCA], [https://pdbe.org/4yvf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4yvf RCSB], [https://www.ebi.ac.uk/pdbsum/4yvf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4yvf ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[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>
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== Function ==
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[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>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Akiko K]]

Current revision

Structure of S-adenosyl-L-homocysteine hydrolase

PDB ID 4yvf

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