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3cus

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==Structure of a double ILE/PHE mutant of NI-FE hydrogenase refined at 2.2 angstrom resolution==
==Structure of a double ILE/PHE mutant of NI-FE hydrogenase refined at 2.2 angstrom resolution==
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<StructureSection load='3cus' size='340' side='right' caption='[[3cus]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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<StructureSection load='3cus' size='340' side='right'caption='[[3cus]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3cus]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Desulfovibrio_fructosovorans Desulfovibrio fructosovorans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CUS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3CUS FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3cus]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Solidesulfovibrio_fructosivorans Solidesulfovibrio fructosivorans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CUS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CUS FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=F3S:FE3-S4+CLUSTER'>F3S</scene>, <scene name='pdbligand=FCO:CARBONMONOXIDE-(DICYANO)+IRON'>FCO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene><br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
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<tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene>, <scene name='pdbligand=F3S:FE3-S4+CLUSTER'>F3S</scene>, <scene name='pdbligand=FCO:CARBONMONOXIDE-(DICYANO)+IRON'>FCO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr>
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<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1frf|1frf]], [[1yrq|1yrq]], [[1yqw|1yqw]], [[3cur|3cur]]</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=3cus FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cus OCA], [https://pdbe.org/3cus PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3cus RCSB], [https://www.ebi.ac.uk/pdbsum/3cus PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3cus ProSAT]</span></td></tr>
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<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">hydA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=878 Desulfovibrio fructosovorans]), hydB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=878 Desulfovibrio fructosovorans])</td></tr>
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</table>
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<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cytochrome-c3_hydrogenase Cytochrome-c3 hydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.12.2.1 1.12.2.1] </span></td></tr>
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== Function ==
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3cus FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cus OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3cus RCSB], [http://www.ebi.ac.uk/pdbsum/3cus PDBsum]</span></td></tr>
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[https://www.uniprot.org/uniprot/PHNS_SOLFR PHNS_SOLFR] Involved in hydrogen uptake for the anaerobic reduction of sulfate to hydrogen sulfide in an electron transport chain. Cytochrome c3 is the physiological electron acceptor.
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<table>
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== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
<jmolCheckbox>
<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cu/3cus_consurf.spt"</scriptWhenChecked>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cu/3cus_consurf.spt"</scriptWhenChecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</jmolCheckbox>
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</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/chain_selection.php?pdb_ID=2ata ConSurf].
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</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=3cus ConSurf].
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<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
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Experimental approaches to kinetics of gas diffusion in hydrogenase.,Leroux F, Dementin S, Burlat B, Cournac L, Volbeda A, Champ S, Martin L, Guigliarelli B, Bertrand P, Fontecilla-Camps J, Rousset M, Leger C Proc Natl Acad Sci U S A. 2008 Aug 12;105(32):11188-93. Epub 2008 Aug 6. PMID:18685111<ref>PMID:18685111</ref>
Experimental approaches to kinetics of gas diffusion in hydrogenase.,Leroux F, Dementin S, Burlat B, Cournac L, Volbeda A, Champ S, Martin L, Guigliarelli B, Bertrand P, Fontecilla-Camps J, Rousset M, Leger C Proc Natl Acad Sci U S A. 2008 Aug 12;105(32):11188-93. Epub 2008 Aug 6. PMID:18685111<ref>PMID:18685111</ref>
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
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<div class="pdbe-citations 3cus" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Cytochrome-c3 hydrogenase]]
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[[Category: Large Structures]]
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[[Category: Desulfovibrio fructosovorans]]
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[[Category: Solidesulfovibrio fructosivorans]]
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[[Category: Volbeda, A.]]
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[[Category: Volbeda A]]
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[[Category: Iron]]
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[[Category: Iron-sulfur]]
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[[Category: Metal-binding]]
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[[Category: Ni-fe hydrogenase tunnel mutant]]
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[[Category: Nickel]]
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[[Category: Oxidoreductase]]
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Current revision

Structure of a double ILE/PHE mutant of NI-FE hydrogenase refined at 2.2 angstrom resolution

PDB ID 3cus

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