3zho

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==X-ray structure of E.coli Wrba in complex with FMN at 1.2 A resolution==
==X-ray structure of E.coli Wrba in complex with FMN at 1.2 A resolution==
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<StructureSection load='3zho' size='340' side='right' caption='[[3zho]], [[Resolution|resolution]] 1.20&Aring;' scene=''>
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<StructureSection load='3zho' size='340' side='right'caption='[[3zho]], [[Resolution|resolution]] 1.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3zho]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZHO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ZHO FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3zho]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZHO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZHO FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene></td></tr>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene></td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SME:METHIONINE+SULFOXIDE'>SME</scene></td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SME:METHIONINE+SULFOXIDE'>SME</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/NAD(P)H_dehydrogenase_(quinone) NAD(P)H dehydrogenase (quinone)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.6.5.2 1.6.5.2] </span></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/NAD(P)H_dehydrogenase_(quinone) NAD(P)H dehydrogenase (quinone)], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.6.5.2 1.6.5.2] </span></td></tr>
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<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=3zho FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zho OCA], [http://pdbe.org/3zho PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3zho RCSB], [http://www.ebi.ac.uk/pdbsum/3zho PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3zho ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3zho FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zho OCA], [https://pdbe.org/3zho PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zho RCSB], [https://www.ebi.ac.uk/pdbsum/3zho PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zho ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/NQOR_ECOLI NQOR_ECOLI]] It seems to function in response to environmental stress when various electron transfer chains are affected or when the environment is highly oxidizing. It reduces quinones to the hydroquinone state to prevent interaction of the semiquinone with O2 and production of superoxide. It prefers NADH over NADPH.<ref>PMID:16672604</ref> <ref>PMID:9694845</ref>
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[[https://www.uniprot.org/uniprot/NQOR_ECOLI NQOR_ECOLI]] It seems to function in response to environmental stress when various electron transfer chains are affected or when the environment is highly oxidizing. It reduces quinones to the hydroquinone state to prevent interaction of the semiquinone with O2 and production of superoxide. It prefers NADH over NADPH.<ref>PMID:16672604</ref> <ref>PMID:9694845</ref>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</StructureSection>
</StructureSection>
[[Category: Bacillus coli migula 1895]]
[[Category: Bacillus coli migula 1895]]
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[[Category: Large Structures]]
[[Category: Brynda, J]]
[[Category: Brynda, J]]
[[Category: Carey, J]]
[[Category: Carey, J]]

Revision as of 05:46, 10 August 2022

X-ray structure of E.coli Wrba in complex with FMN at 1.2 A resolution

PDB ID 3zho

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