5jfc: Difference between revisions
New page: '''Unreleased structure''' The entry 5jfc is ON HOLD Authors: Zadvornyy, O.A., Schut, G.J., Nguyen, D.M., Artz, J.H., Tokmina-Lukaszewska, M., Lipscomb, G., Adams, M.W., Peters, J.W. D... |
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==NADH-dependent Ferredoxin:NADP Oxidoreductase (NfnI) from Pyrococcus furiosus== | |||
<StructureSection load='5jfc' size='340' side='right'caption='[[5jfc]], [[Resolution|resolution]] 1.60Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5jfc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JFC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5JFC FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.598Å</td></tr> | |||
[[Category: | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr> | ||
[[Category: | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5jfc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jfc OCA], [https://pdbe.org/5jfc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5jfc RCSB], [https://www.ebi.ac.uk/pdbsum/5jfc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5jfc ProSAT]</span></td></tr> | ||
[[Category: | </table> | ||
[[Category: Artz | == Function == | ||
[[Category: | [https://www.uniprot.org/uniprot/SUDHA_PYRFU SUDHA_PYRFU] A bifunctional enzyme that catalyzes the reduction of elemental sulfur or polysulfide to hydrogen sulfide with NADPH as electron donor. Also functions as a reduced ferredoxin:NADP oxidoreductase with a very high affinity for reduced ferredoxin. Exhibits a broad specificity for various physiological and non-physiological substrates with varied reduction potentials such as methyl viologen, benzyl viologen, FAD, FMN, methylene blue, 2,6-dichlorophenolindophenol (DCIP), cytochrome C and ferricyanide with highest preference for benzyl viologen. Does not reduce fumarate, succinate, nitrate, nitrite, sulfate, sulfite or protons. Does not possess any hydrogenase activity or NADPH-dependent glutamate synthase activity.<ref>PMID:10968624</ref> <ref>PMID:7961401</ref> [REFERENCE:4] | ||
[[Category: | == References == | ||
[[Category: | <references/> | ||
[[Category: | __TOC__ | ||
[[Category: Tokmina-Lukaszewska | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Pyrococcus furiosus]] | |||
[[Category: Adams MW]] | |||
[[Category: Artz JH]] | |||
[[Category: King PW]] | |||
[[Category: Lipscomb G]] | |||
[[Category: Nguyen DM]] | |||
[[Category: Peters JW]] | |||
[[Category: Schut GJ]] | |||
[[Category: Tokmina-Lukaszewska M]] | |||
[[Category: Zadvornyy OA]] |
Latest revision as of 15:37, 6 March 2024
NADH-dependent Ferredoxin:NADP Oxidoreductase (NfnI) from Pyrococcus furiosusNADH-dependent Ferredoxin:NADP Oxidoreductase (NfnI) from Pyrococcus furiosus
Structural highlights
FunctionSUDHA_PYRFU A bifunctional enzyme that catalyzes the reduction of elemental sulfur or polysulfide to hydrogen sulfide with NADPH as electron donor. Also functions as a reduced ferredoxin:NADP oxidoreductase with a very high affinity for reduced ferredoxin. Exhibits a broad specificity for various physiological and non-physiological substrates with varied reduction potentials such as methyl viologen, benzyl viologen, FAD, FMN, methylene blue, 2,6-dichlorophenolindophenol (DCIP), cytochrome C and ferricyanide with highest preference for benzyl viologen. Does not reduce fumarate, succinate, nitrate, nitrite, sulfate, sulfite or protons. Does not possess any hydrogenase activity or NADPH-dependent glutamate synthase activity.[1] [2] [REFERENCE:4] References
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