5h7d: Difference between revisions

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 ==Crystal structure of the YgjG-protein A-Zpa963-calmodulin complex==
-<StructureSection load='5h7d' size='340' side='right' caption='[[5h7d]], [[Resolution|resolution]] 2.57&Aring;' scene=''>
+<StructureSection load='5h7d' size='340' side='right'caption='[[5h7d]], [[Resolution|resolution]] 2.57&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5h7d]] is a 16 chain structure with sequence from [http://en.wikipedia.org/wiki/"micrococcus_aureus"_(rosenbach_1884)_zopf_1885 "micrococcus aureus" (rosenbach 1884) zopf 1885] and [http://en.wikipedia.org/wiki/Synthetic_construct_sequences Synthetic construct sequences]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5H7D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5H7D FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5h7d]] is a 16 chain structure with sequence from [https://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans], [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12], [https://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5H7D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5H7D FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</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]] 2.57&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5h75|5h75]], [[5h76|5h76]], [[5h77|5h77]], [[5h78|5h78]], [[5h79|5h79]], [[5h7a|5h7a]], [[5h7b|5h7b]], [[5h7c|5h7c]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">spa ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1280 "Micrococcus aureus" (Rosenbach 1884) Zopf 1885]), cmd-1, T21H3.3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=32630 SYNTHETIC CONSTRUCT sequences])</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=5h7d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5h7d OCA], [https://pdbe.org/5h7d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5h7d RCSB], [https://www.ebi.ac.uk/pdbsum/5h7d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5h7d ProSAT]</span></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Putrescine_aminotransferase Putrescine aminotransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.82 2.6.1.82] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5h7d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5h7d OCA], [http://pdbe.org/5h7d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5h7d RCSB], [http://www.ebi.ac.uk/pdbsum/5h7d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5h7d ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/PAT_ECOLI PAT_ECOLI]] Catalyzes the aminotransferase reaction from putrescine to 2-oxoglutarate, leading to glutamate and 4-aminobutanal, which spontaneously cyclizes to form 1-pyrroline. Is also able to transaminate cadaverine and, in lower extent, spermidine, but not ornithine. Alpha-ketobutyrate and pyruvate can also act as amino acceptors, although much less efficiently.<ref>PMID:12617754</ref>
+[https://www.uniprot.org/uniprot/PAT_ECOLI PAT_ECOLI] Catalyzes the aminotransferase reaction from putrescine to 2-oxoglutarate, leading to glutamate and 4-aminobutanal, which spontaneously cyclizes to form 1-pyrroline. Is also able to transaminate cadaverine and, in lower extent, spermidine, but not ornithine. Alpha-ketobutyrate and pyruvate can also act as amino acceptors, although much less efficiently.<ref>PMID:12617754</ref> [https://www.uniprot.org/uniprot/SPA_STAAU SPA_STAAU]
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 25: / Line 23: @@
 __TOC__
 </StructureSection>
-[[Category: Putrescine aminotransferase]]
+[[Category: Caenorhabditis elegans]]
-[[Category: Synthetic construct sequences]]
+[[Category: Escherichia coli K-12]]
-[[Category: Kim, J H]]
+[[Category: Large Structures]]
-[[Category: Kwon, N Y]]
+[[Category: Staphylococcus aureus]]
-[[Category: Lee, H]]
+[[Category: Synthetic construct]]
-[[Category: Lee, J H]]
+[[Category: Kim JH]]
-[[Category: Lee, J O]]
+[[Category: Kwon NY]]
-[[Category: Youn, S J]]
+[[Category: Lee H]]
-[[Category: Immune system-metal binding protein complex]]
+[[Category: Lee JH]]
-[[Category: Synthetic protein]]
+[[Category: Lee JO]]
-[[Category: Transferase]]
+[[Category: Youn SJ]]