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3u7q

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3u7q]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3U7Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3U7Q FirstGlance]. <br>
<table><tr><td colspan='2'>[[3u7q]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3U7Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3U7Q FirstGlance]. <br>
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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=1CL:FE(8)-S(7)+CLUSTER,+OXIDIZED'>1CL</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CLF:FE(8)-S(7)+CLUSTER'>CLF</scene>, <scene name='pdbligand=HCA:3-HYDROXY-3-CARBOXY-ADIPIC+ACID'>HCA</scene>, <scene name='pdbligand=ICS:IRON-SULFUR-MOLYBDENUM+CLUSTER+WITH+INTERSTITIAL+CARBON'>ICS</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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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]] 1&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1m1n|1m1n]], [[1min|1min]]</div></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=1CL:FE(8)-S(7)+CLUSTER,+OXIDIZED'>1CL</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CLF:FE(8)-S(7)+CLUSTER'>CLF</scene>, <scene name='pdbligand=HCA:3-HYDROXY-3-CARBOXY-ADIPIC+ACID'>HCA</scene>, <scene name='pdbligand=ICS:IRON-SULFUR-MOLYBDENUM+CLUSTER+WITH+INTERSTITIAL+CARBON'>ICS</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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/Nitrogenase Nitrogenase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.18.6.1 1.18.6.1] </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=3u7q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u7q OCA], [https://pdbe.org/3u7q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3u7q RCSB], [https://www.ebi.ac.uk/pdbsum/3u7q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3u7q ProSAT]</span></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=3u7q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u7q OCA], [https://pdbe.org/3u7q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3u7q RCSB], [https://www.ebi.ac.uk/pdbsum/3u7q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3u7q ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/NIFD_AZOVI NIFD_AZOVI]] This molybdenum-iron protein is part of the nitrogenase complex that catalyzes the key enzymatic reactions in nitrogen fixation. [[https://www.uniprot.org/uniprot/NIFK_AZOVI NIFK_AZOVI]] This molybdenum-iron protein is part of the nitrogenase complex that catalyzes the key enzymatic reactions in nitrogen fixation.
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[https://www.uniprot.org/uniprot/NIFK_AZOVI NIFK_AZOVI] This molybdenum-iron protein is part of the nitrogenase complex that catalyzes the key enzymatic reactions in nitrogen fixation.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The identity of the interstitial light atom in the center of the FeMo cofactor of nitrogenase has been enigmatic since its discovery. Atomic-resolution x-ray diffraction data and an electron spin echo envelope modulation (ESEEM) analysis now provide direct evidence that the ligand is a carbon species.
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Evidence for interstitial carbon in nitrogenase FeMo cofactor.,Spatzal T, Aksoyoglu M, Zhang L, Andrade SL, Schleicher E, Weber S, Rees DC, Einsle O Science. 2011 Nov 18;334(6058):940. PMID:22096190<ref>PMID:22096190</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3u7q" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Nitrogenase 3D structures|Nitrogenase 3D structures]]
*[[Nitrogenase 3D structures|Nitrogenase 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Azotobacter vinelandii]]
[[Category: Azotobacter vinelandii]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Nitrogenase]]
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[[Category: Einsle O]]
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[[Category: Einsle, O]]
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[[Category: Spatzal T]]
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[[Category: Spatzal, T]]
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[[Category: Multiple rossmann fold domain]]
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[[Category: Nitrogen fixing]]
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[[Category: Oxidoreductase]]
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[[Category: Reductase]]
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Current revision

A. vinelandii nitrogenase MoFe protein at atomic resolution

PDB ID 3u7q

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