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New page: left|200px<br /><applet load="2cb1" size="350" color="white" frame="true" align="right" spinBox="true" caption="2cb1, resolution 2.00Å" /> '''CRYSTAL STRUCTURE OF... |
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== | ==Crystal Structure of O-actetyl Homoserine Sulfhydrylase From Thermus Thermophilus HB8,OAH2.== | ||
<StructureSection load='2cb1' size='340' side='right'caption='[[2cb1]], [[Resolution|resolution]] 2.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2cb1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB8 Thermus thermophilus HB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CB1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CB1 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</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=2cb1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cb1 OCA], [https://pdbe.org/2cb1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cb1 RCSB], [https://www.ebi.ac.uk/pdbsum/2cb1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cb1 ProSAT], [https://www.topsan.org/Proteins/RSGI/2cb1 TOPSAN]</span></td></tr> | ||
[[ | </table> | ||
[ | == Function == | ||
[[ | [https://www.uniprot.org/uniprot/METY2_THET8 METY2_THET8] Catalyzes the conversion of O-acetyl-L-homoserine (OAH) into homocysteine in the methionine biosynthesis pathway. Has weak activity with O-acetyl-L-serine, O-phospho-L-serine, L-serine, O-succinyl-L-homoserine and L-homoserine. Shows a very low CTT gamma-synthase activity.<ref>PMID:15215603</ref> | ||
[ | == Evolutionary Conservation == | ||
[[Category: | [[Image:Consurf_key_small.gif|200px|right]] | ||
[[Category: | Check<jmol> | ||
[[Category: | <jmolCheckbox> | ||
[[Category: | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cb/2cb1_consurf.spt"</scriptWhenChecked> | ||
[[Category: | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
[[Category: | <text>to colour the structure by Evolutionary Conservation</text> | ||
[[Category: | </jmolCheckbox> | ||
[[Category: | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2cb1 ConSurf]. | ||
[[Category: | <div style="clear:both"></div> | ||
[[Category: | == References == | ||
[[Category: | <references/> | ||
[[Category: | __TOC__ | ||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Thermus thermophilus HB8]] | |||
[[Category: Agari Y]] | |||
[[Category: Ebihara A]] | |||
[[Category: Imagawa T]] | |||
[[Category: Kanagawa M]] | |||
[[Category: Kuramitsu S]] | |||
[[Category: Kuroishi C]] | |||
[[Category: Nakagawa N]] | |||
[[Category: Tsuge H]] | |||
[[Category: Utsunomiya H]] | |||
[[Category: Yokoyama S]] | |||
Latest revision as of 17:11, 13 December 2023
Crystal Structure of O-actetyl Homoserine Sulfhydrylase From Thermus Thermophilus HB8,OAH2.Crystal Structure of O-actetyl Homoserine Sulfhydrylase From Thermus Thermophilus HB8,OAH2.
Structural highlights
FunctionMETY2_THET8 Catalyzes the conversion of O-acetyl-L-homoserine (OAH) into homocysteine in the methionine biosynthesis pathway. Has weak activity with O-acetyl-L-serine, O-phospho-L-serine, L-serine, O-succinyl-L-homoserine and L-homoserine. Shows a very low CTT gamma-synthase activity.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. References
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