6ymd: Difference between revisions

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 <StructureSection load='6ymd' size='340' side='right'caption='[[6ymd]], [[Resolution|resolution]] 1.25&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6ymd]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Aphha Aphha]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6YMD OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6YMD FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6ymd]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aphanothece_halophytica Aphanothece halophytica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6YMD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6YMD FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MLI:MALONATE+ION'>MLI</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PMP:4-DEOXY-4-AMINOPYRIDOXAL-5-PHOSPHATE'>PMP</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]] 1.25&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">glyrA, glyA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=72020 APHHA])</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MLI:MALONATE+ION'>MLI</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PMP:4-DEOXY-4-AMINOPYRIDOXAL-5-PHOSPHATE'>PMP</scene></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glycine_hydroxymethyltransferase Glycine hydroxymethyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.2.1 2.1.2.1] </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=6ymd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ymd OCA], [https://pdbe.org/6ymd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ymd RCSB], [https://www.ebi.ac.uk/pdbsum/6ymd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ymd ProSAT]</span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6ymd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ymd OCA], [http://pdbe.org/6ymd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ymd RCSB], [http://www.ebi.ac.uk/pdbsum/6ymd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ymd ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/I7H6W6_APHHA I7H6W6_APHHA]] Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism.[HAMAP-Rule:MF_00051]
+[https://www.uniprot.org/uniprot/I7H6W6_APHHA I7H6W6_APHHA] Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism.[HAMAP-Rule:MF_00051]
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
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 </div>
 <div class="pdbe-citations 6ymd" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Serine hydroxymethyltransferase 3D structures|Serine hydroxymethyltransferase 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Aphha]]
+[[Category: Aphanothece halophytica]]
-[[Category: Glycine hydroxymethyltransferase]]
 [[Category: Large Structures]]
-[[Category: Angelaccio, S]]
+[[Category: Angelaccio S]]
-[[Category: Contestabile, R]]
+[[Category: Contestabile R]]
-[[Category: Nogues, I]]
+[[Category: Nogues I]]
-[[Category: Ruszkowski, M]]
+[[Category: Ruszkowski M]]
-[[Category: Sekula, B]]
+[[Category: Sekula B]]
-[[Category: Tramonti, A]]
+[[Category: Tramonti A]]
-[[Category: Glycine]]
-[[Category: One-carbon metabolism]]
-[[Category: Plp]]
-[[Category: Serine biosynthesis]]
-[[Category: Tetrahydrofolate]]
-[[Category: Transferase]]