1m1n: Difference between revisions

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 <StructureSection load='1m1n' size='340' side='right'caption='[[1m1n]], [[Resolution|resolution]] 1.16&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1m1n]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_478 Atcc 478]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M1N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1M1N FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1m1n]] is a 8 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=1M1N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1M1N FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CFN:FE(7)-MO-S(9)-N+CLUSTER'>CFN</scene>, <scene name='pdbligand=CLF:FE(8)-S(7)+CLUSTER'>CLF</scene>, <scene name='pdbligand=HCA:3-HYDROXY-3-CARBOXY-ADIPIC+ACID'>HCA</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.16&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3min|3min]], [[2min|2min]], [[1n2c|1n2c]]</div></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CFN:FE(7)-MO-S(9)-N+CLUSTER'>CFN</scene>, <scene name='pdbligand=CLF:FE(8)-S(7)+CLUSTER'>CLF</scene>, <scene name='pdbligand=HCA:3-HYDROXY-3-CARBOXY-ADIPIC+ACID'>HCA</scene></td></tr>
-<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>
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1m1n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m1n OCA], [https://pdbe.org/1m1n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1m1n RCSB], [https://www.ebi.ac.uk/pdbsum/1m1n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1m1n ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[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.
+[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.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
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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=1m1n ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-A high-resolution crystallographic analysis of the nitrogenase MoFe-protein reveals a previously unrecognized ligand coordinated to six iron atoms in the center of the catalytically essential FeMo-cofactor. The electron density for this ligand is masked in structures with resolutions lower than 1.55 angstroms, owing to Fourier series termination ripples from the surrounding iron and sulfur atoms in the cofactor. The central atom completes an approximate tetrahedral coordination for the six iron atoms, instead of the trigonal coordination proposed on the basis of lower resolution structures. The crystallographic refinement at 1.16 angstrom resolution is consistent with this newly detected component being a light element, most plausibly nitrogen. The presence of a nitrogen atom in the cofactor would have important implications for the mechanism of dinitrogen reduction by nitrogenase.
-Nitrogenase MoFe-protein at 1.16 A resolution: a central ligand in the FeMo-cofactor.,Einsle O, Tezcan FA, Andrade SL, Schmid B, Yoshida M, Howard JB, Rees DC Science. 2002 Sep 6;297(5587):1696-700. PMID:12215645<ref>PMID:12215645</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1m1n" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Nitrogenase 3D structures|Nitrogenase 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Atcc 478]]
+[[Category: Azotobacter vinelandii]]
 [[Category: Large Structures]]
-[[Category: Nitrogenase]]
+[[Category: Andrade SLA]]
-[[Category: Andrade, S L.A]]
+[[Category: Einsle O]]
-[[Category: Einsle, O]]
+[[Category: Howard JB]]
-[[Category: Howard, J B]]
+[[Category: Rees DC]]
-[[Category: Rees, D C]]
+[[Category: Schmid B]]
-[[Category: Schmid, B]]
+[[Category: Tezcan FA]]
-[[Category: Tezcan, F A]]
+[[Category: Yoshida M]]
-[[Category: Yoshida, M]]
-[[Category: Atomic resolution]]
-[[Category: Central nitrogen ligand]]
-[[Category: Femo cofactor]]
-[[Category: Nitrogen fixation]]
-[[Category: Oxidoreductase]]