1vlv: Difference between revisions
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<StructureSection load='1vlv' size='340' side='right'caption='[[1vlv]], [[Resolution|resolution]] 2.25Å' scene=''> | <StructureSection load='1vlv' size='340' side='right'caption='[[1vlv]], [[Resolution|resolution]] 2.25Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1vlv]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1vlv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VLV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VLV FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.25Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></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=1vlv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vlv OCA], [https://pdbe.org/1vlv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vlv RCSB], [https://www.ebi.ac.uk/pdbsum/1vlv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vlv ProSAT], [https://www.topsan.org/Proteins/JCSG/1vlv TOPSAN]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/OTC_THEMA OTC_THEMA] Reversibly catalyzes the transfer of the carbamoyl group from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to produce L-citrulline, which is a substrate for argininosuccinate synthetase, the enzyme involved in the final step in arginine biosynthesis (By similarity). | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Thermotoga maritima]] | ||
Latest revision as of 17:53, 20 September 2023
Crystal structure of Ornithine carbamoyltransferase (TM1097) from Thermotoga maritima at 2.25 A resolutionCrystal structure of Ornithine carbamoyltransferase (TM1097) from Thermotoga maritima at 2.25 A resolution
Structural highlights
FunctionOTC_THEMA Reversibly catalyzes the transfer of the carbamoyl group from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to produce L-citrulline, which is a substrate for argininosuccinate synthetase, the enzyme involved in the final step in arginine biosynthesis (By similarity). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. See Also |
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