2dyu: Difference between revisions
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==Helicobacter pylori formamidase AmiF contains a fine-tuned cysteine-glutamate-lysine catalytic triad== | |||
<StructureSection load='2dyu' size='340' side='right'caption='[[2dyu]], [[Resolution|resolution]] 1.75Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2dyu]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Helicobacter_pylori_26695 Helicobacter pylori 26695]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DYU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2DYU 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]] 1.75Å</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=2dyu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dyu OCA], [https://pdbe.org/2dyu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2dyu RCSB], [https://www.ebi.ac.uk/pdbsum/2dyu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2dyu ProSAT]</span></td></tr> | |||
== | </table> | ||
[[2dyu]] is a 2 chain structure with sequence from [ | == Function == | ||
[https://www.uniprot.org/uniprot/AMIF_HELPY AMIF_HELPY] Is an aliphatic amidase with a restricted substrate specificity, as it only hydrolyzes formamide. Probably involved in the nitrogen metabolism of H.pylori.<ref>PMID:11359566</ref> | |||
== | == Evolutionary Conservation == | ||
< | [[Image:Consurf_key_small.gif|200px|right]] | ||
[[ | Check<jmol> | ||
[[ | <jmolCheckbox> | ||
[ | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dy/2dyu_consurf.spt"</scriptWhenChecked> | ||
[[ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
[ | <text>to colour the structure by Evolutionary Conservation</text> | ||
[[ | </jmolCheckbox> | ||
[ | </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=2dyu ConSurf]. | ||
[[Category: | <div style="clear:both"></div> | ||
[[Category: | == References == | ||
[[Category: | <references/> | ||
[[Category: | __TOC__ | ||
</StructureSection> | |||
[[Category: Helicobacter pylori 26695]] | |||
[[Category: Large Structures]] | |||
[[Category: Hung CL]] | |||
[[Category: Wang WC]] | |||
Latest revision as of 16:48, 13 March 2024
Helicobacter pylori formamidase AmiF contains a fine-tuned cysteine-glutamate-lysine catalytic triadHelicobacter pylori formamidase AmiF contains a fine-tuned cysteine-glutamate-lysine catalytic triad
Structural highlights
FunctionAMIF_HELPY Is an aliphatic amidase with a restricted substrate specificity, as it only hydrolyzes formamide. Probably involved in the nitrogen metabolism of H.pylori.[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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