2obv: Difference between revisions

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 <StructureSection load='2obv' size='340' side='right'caption='[[2obv]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2obv]] is a 1 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=2OBV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OBV FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2obv]] is a 1 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=2OBV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OBV FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</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]] 2.05&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MAT1A, AMS1, MATA1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Methionine_adenosyltransferase Methionine adenosyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.6 2.5.1.6] </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=2obv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2obv OCA], [https://pdbe.org/2obv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2obv RCSB], [https://www.ebi.ac.uk/pdbsum/2obv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2obv ProSAT]</span></td></tr>
 </table>
 == Disease ==
-[[https://www.uniprot.org/uniprot/METK1_HUMAN METK1_HUMAN]] Defects in MAT1A are the cause of methionine adenosyltransferase deficiency (MATD) [MIM:[https://omim.org/entry/250850 250850]]; also called MAT I/III deficiency. MATD is an inborn error of metabolism resulting in isolated hypermethioninemia. Most patients have no clinical abnormalities, although some neurologic symptoms may be present in rare cases with severe loss of methionine adenosyltransferase activity.<ref>PMID:7560086</ref> <ref>PMID:8770875</ref> <ref>PMID:9042912</ref> <ref>PMID:10677294</ref>
+[https://www.uniprot.org/uniprot/METK1_HUMAN METK1_HUMAN] Defects in MAT1A are the cause of methionine adenosyltransferase deficiency (MATD) [MIM:[https://omim.org/entry/250850 250850]; also called MAT I/III deficiency. MATD is an inborn error of metabolism resulting in isolated hypermethioninemia. Most patients have no clinical abnormalities, although some neurologic symptoms may be present in rare cases with severe loss of methionine adenosyltransferase activity.<ref>PMID:7560086</ref> <ref>PMID:8770875</ref> <ref>PMID:9042912</ref> <ref>PMID:10677294</ref>
 == Function ==
-[[https://www.uniprot.org/uniprot/METK1_HUMAN METK1_HUMAN]] Catalyzes the formation of S-adenosylmethionine from methionine and ATP.
+[https://www.uniprot.org/uniprot/METK1_HUMAN METK1_HUMAN] Catalyzes the formation of S-adenosylmethionine from methionine and ATP.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 25: / Line 24: @@
 ==See Also==
-*[[SAM synthetase|SAM synthetase]]
+*[[Methionine adenosyltransferase|Methionine adenosyltransferase]]
+*[[S-adenosylmethionine synthetase 3D structures|S-adenosylmethionine synthetase 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Methionine adenosyltransferase]]
+[[Category: Arrowsmith CH]]
-[[Category: Arrowsmith, C H]]
+[[Category: Cooper C]]
-[[Category: Cooper, C]]
+[[Category: Edwards A]]
-[[Category: Delft, F von]]
+[[Category: Hozjan V]]
-[[Category: Edwards, A]]
+[[Category: Kavanagh KL]]
-[[Category: Hozjan, V]]
+[[Category: Oppermann U]]
-[[Category: Kavanagh, K L]]
+[[Category: Pilka ES]]
-[[Category: Oppermann, U]]
+[[Category: Shafqat N]]
-[[Category: Pilka, E S]]
+[[Category: Sundstrom M]]
-[[Category: Structural genomic]]
+[[Category: Turnbull A]]
-[[Category: Shafqat, N]]
+[[Category: Weigelt J]]
-[[Category: Sundstrom, M]]
+[[Category: Von Delft F]]
-[[Category: Turnbull, A]]
-[[Category: Weigelt, J]]
-[[Category: Sgc]]
-[[Category: Synthetase]]
-[[Category: Transferase]]