3k1a

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Current revision (08:07, 6 September 2023) (edit) (undo)
 
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<StructureSection load='3k1a' size='340' side='right'caption='[[3k1a]], [[Resolution|resolution]] 2.23&Aring;' scene=''>
<StructureSection load='3k1a' size='340' side='right'caption='[[3k1a]], [[Resolution|resolution]] 2.23&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3k1a]] is a 4 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=3K1A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3K1A FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3k1a]] 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=3K1A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3K1A 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=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>
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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]] 2.23&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">nifDK, nifK ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=354 ATCC 478]), nifD ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=354 ATCC 478])</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=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>
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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=3k1a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3k1a OCA], [https://pdbe.org/3k1a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3k1a RCSB], [https://www.ebi.ac.uk/pdbsum/3k1a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3k1a 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=3k1a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3k1a OCA], [https://pdbe.org/3k1a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3k1a RCSB], [https://www.ebi.ac.uk/pdbsum/3k1a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3k1a 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/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 ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Atcc 478]]
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[[Category: Azotobacter vinelandii]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Nitrogenase]]
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[[Category: Barney BM]]
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[[Category: Barney, B M]]
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[[Category: Dean DR]]
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[[Category: Dean, D R]]
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[[Category: Keable S]]
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[[Category: Keable, S]]
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[[Category: Peters JW]]
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[[Category: Peters, J W]]
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[[Category: Sarma R]]
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[[Category: Sarma, R]]
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[[Category: Seefeldt LC]]
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[[Category: Seefeldt, L C]]
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[[Category: Acetylene]]
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[[Category: Atp-binding]]
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[[Category: Hydride reduction]]
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[[Category: Iron]]
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[[Category: Iron-sulfur]]
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[[Category: Isoleucine]]
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[[Category: Metal-binding]]
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[[Category: Mofe protein]]
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[[Category: Molybdenum]]
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[[Category: Nitrogen]]
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[[Category: Nitrogen fixation]]
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[[Category: Nucleotide-binding]]
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[[Category: Oxidoreductase]]
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[[Category: Proton reduction]]
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Current revision

Insights into substrate binding at FeMo-cofactor in nitrogenase from the structure of an alpha-70Ile MoFe protein variant

PDB ID 3k1a

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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