1h4t: Difference between revisions

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 <StructureSection load='1h4t' size='340' side='right'caption='[[1h4t]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1h4t]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H4T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1H4T FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1h4t]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H4T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H4T FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PRO:PROLINE'>PRO</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 2.9&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1h4q|1h4q]], [[1h4s|1h4s]], [[1hc7|1hc7]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PRO:PROLINE'>PRO</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Proline--tRNA_ligase Proline--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.15 6.1.1.15] </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=1h4t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h4t OCA], [https://pdbe.org/1h4t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h4t RCSB], [https://www.ebi.ac.uk/pdbsum/1h4t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h4t ProSAT]</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=1h4t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h4t OCA], [http://pdbe.org/1h4t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1h4t RCSB], [http://www.ebi.ac.uk/pdbsum/1h4t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1h4t ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/SYP_THET8 SYP_THET8] Catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). Can inadvertently accommodate and process cysteine.<ref>PMID:12013438</ref> <ref>PMID:12130657</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 36: / Line 37: @@
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Proline--tRNA ligase]]
 [[Category: Thermus thermophilus]]
-[[Category: Cusack, S]]
+[[Category: Cusack S]]
-[[Category: Tukalo, M]]
+[[Category: Tukalo M]]
-[[Category: Yaremchuk, A]]
+[[Category: Yaremchuk A]]
-[[Category: Aminoacyl-trna synthetase]]
-[[Category: Class ii aminoacyl-trna synthetase]]