5jca - Revision history

OCA at 12:23, 13 August 2026

2026-08-13T12:23:26Z

← Older revision		Revision as of 12:23, 13 August 2026
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	<table><tr><td colspan='2'>[[5jca]] 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=5JCA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5JCA FirstGlance]. <br>		<table><tr><td colspan='2'>[[5jca]] 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=5JCA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5JCA 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]] 1.5Å</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]] 1.5Å</td></tr>
	<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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP~~</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4~~</scene></td></tr>		<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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene></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=5jca FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jca OCA], [https://pdbe.org/5jca PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5jca RCSB], [https://www.ebi.ac.uk/pdbsum/5jca PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5jca 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=5jca FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jca OCA], [https://pdbe.org/5jca PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5jca RCSB], [https://www.ebi.ac.uk/pdbsum/5jca PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5jca ProSAT]</span></td></tr>
	</table>		</table>

OCA at 12:58, 20 December 2023

2023-12-20T12:58:17Z

← Older revision		Revision as of 12:58, 20 December 2023
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[5jca]] 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=5JCA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5JCA FirstGlance]. <br>		<table><tr><td colspan='2'>[[5jca]] 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=5JCA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5JCA FirstGlance]. <br>
	</td></tr><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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</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]] 1.5Å</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/NAD(P)(+)_transhydrogenase_(ferredoxin) NAD(P)(+) transhydrogenase (ferredoxin)], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.6.1.4 1.6.1.4] </span></td></tr>		<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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></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=5jca FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jca OCA], [https://pdbe.org/5jca PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5jca RCSB], [https://www.ebi.ac.uk/pdbsum/5jca PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5jca 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=5jca FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jca OCA], [https://pdbe.org/5jca PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5jca RCSB], [https://www.ebi.ac.uk/pdbsum/5jca PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5jca ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[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] [[https://www.uniprot.org/uniprot/SUDHB_PYRFU SUDHB_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> <ref>PMID:7961401</ref>		[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]
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Pyrococcus furiosus]]		[[Category: Pyrococcus furiosus]]
	[[Category: Adams~~, M W~~]]		[[Category: Adams MW]]
	[[Category: Artz~~, J H~~]]		[[Category: Artz JH]]
	[[Category: Lipscomb, G]]		[[Category: Lipscomb G]]
	[[Category: Nguyen~~, D M~~]]		[[Category: Nguyen DM]]
	[[Category: Peters~~, J W~~]]		[[Category: Peters JW]]
	[[Category: Schut~~, G J~~]]		[[Category: Schut GJ]]
	[[Category: Tokmina-Lukaszewska, M]]		[[Category: Tokmina-Lukaszewska M]]
	[[Category: Zadvornyy~~, O A]]~~		[[Category: Zadvornyy OA]]
	~~[[Category: Nfni]]~~
	~~[[Category: Oxidoreductase~~]]

OCA at 07:06, 16 March 2022

2022-03-16T07:06:11Z

← Older revision		Revision as of 07:06, 16 March 2022
Line 3:		Line 3:
	<StructureSection load='5jca' size='340' side='right'caption='[[5jca]], [[Resolution\|resolution]] 1.50Å' scene=''>		<StructureSection load='5jca' size='340' side='right'caption='[[5jca]], [[Resolution\|resolution]] 1.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[5jca]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JCA OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=5JCA FirstGlance]. <br>		<table><tr><td colspan='2'>[[5jca]] 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=5JCA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5JCA FirstGlance]. <br>
	</td></tr><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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr>		</td></tr><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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/NAD(P)(+)_transhydrogenase_(ferredoxin) NAD(P)(+) transhydrogenase (ferredoxin)], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.6.1.4 1.6.1.4] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/NAD(P)(+)_transhydrogenase_(ferredoxin) NAD(P)(+) transhydrogenase (ferredoxin)], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.6.1.4 1.6.1.4] </span></td></tr>
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=5jca FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jca OCA], [~~http~~://pdbe.org/5jca PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5jca RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5jca PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5jca 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=5jca FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jca OCA], [https://pdbe.org/5jca PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5jca RCSB], [https://www.ebi.ac.uk/pdbsum/5jca PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5jca ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[~~http~~://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] [[~~http~~://www.uniprot.org/uniprot/SUDHB_PYRFU SUDHB_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> <ref>PMID:7961401</ref>		[[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] [[https://www.uniprot.org/uniprot/SUDHB_PYRFU SUDHB_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> <ref>PMID:7961401</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 07:41, 10 June 2020

2020-06-10T07:41:48Z

← Older revision		Revision as of 07:41, 10 June 2020
Line 1:		Line 1:

	==NADP(H) bound NADH-dependent Ferredoxin:NADP Oxidoreductase (NfnI) from Pyrococcus furiosus==		==NADP(H) bound NADH-dependent Ferredoxin:NADP Oxidoreductase (NfnI) from Pyrococcus furiosus==
	<StructureSection load='5jca' size='340' side='right' caption='[[5jca]], [[Resolution\|resolution]] 1.50Å' scene=''>		<StructureSection load='5jca' size='340' side='right'caption='[[5jca]], [[Resolution\|resolution]] 1.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[5jca]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JCA OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5JCA FirstGlance]. <br>		<table><tr><td colspan='2'>[[5jca]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JCA OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5JCA FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr>		</td></tr><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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/NAD(P)(+)_transhydrogenase_(ferredoxin) NAD(P)(+) transhydrogenase (ferredoxin)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.6.1.4 1.6.1.4] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/NAD(P)(+)_transhydrogenase_(ferredoxin) NAD(P)(+) transhydrogenase (ferredoxin)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.6.1.4 1.6.1.4] </span></td></tr>
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5jca FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jca OCA], [http://pdbe.org/5jca PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5jca RCSB], [http://www.ebi.ac.uk/pdbsum/5jca PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5jca ProSAT]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5jca FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jca OCA], [http://pdbe.org/5jca PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5jca RCSB], [http://www.ebi.ac.uk/pdbsum/5jca PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5jca ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 23:		Line 23:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
			[[Category: Large Structures]]
	[[Category: Pyrococcus furiosus]]		[[Category: Pyrococcus furiosus]]
	[[Category: Adams, M W]]		[[Category: Adams, M W]]

OCA at 07:40, 27 April 2017

2017-04-27T07:40:02Z

← Older revision		Revision as of 07:40, 27 April 2017
Line 10:		Line 10:
	== Function ==		== Function ==
	[[http://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] [[http://www.uniprot.org/uniprot/SUDHB_PYRFU SUDHB_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> <ref>PMID:7961401</ref>		[[http://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] [[http://www.uniprot.org/uniprot/SUDHB_PYRFU SUDHB_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> <ref>PMID:7961401</ref>
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			The recently realized biochemical phenomenon of energy conservation through electron bifurcation provides biology with an elegant means to maximize utilization of metabolic energy. The mechanism of coordinated coupling of exergonic and endergonic oxidation-reduction reactions by a single enzyme complex has been elucidated through optical and paramagnetic spectroscopic studies revealing unprecedented features. Pairs of electrons are bifurcated over more than 1 volt of electrochemical potential by generating a low-potential, highly energetic, unstable flavin semiquinone and directing electron flow to an iron-sulfur cluster with a highly negative potential to overcome the barrier of the endergonic half reaction. The unprecedented range of thermodynamic driving force that is generated by flavin-based electron bifurcation accounts for unique chemical reactions that are catalyzed by these enzymes.

			Mechanistic insights into energy conservation by flavin-based electron bifurcation.,Lubner CE, Jennings DP, Mulder DW, Schut GJ, Zadvornyy OA, Hoben JP, Tokmina-Lukaszewska M, Berry L, Nguyen DM, Lipscomb GL, Bothner B, Jones AK, Miller AF, King PW, Adams MWW, Peters JW Nat Chem Biol. 2017 Apr 10. doi: 10.1038/nchembio.2348. PMID:28394885<ref>PMID:28394885</ref>

			From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>
			<div class="pdbe-citations 5jca" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 11:43, 12 April 2017

2017-04-12T11:43:08Z

← Older revision		Revision as of 11:43, 12 April 2017
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	~~'''Unreleased structure'''~~

	~~The entry~~ 5jca ~~is ON HOLD until Paper Publication~~		==NADP(H) bound NADH-dependent Ferredoxin:NADP Oxidoreductase (NfnI) from Pyrococcus furiosus==
			<StructureSection load='5jca' size='340' side='right' caption='[[5jca]], [[Resolution\|resolution]] 1.50Å' scene=''>
	~~Authors~~: ~~Zadvornyy, O~~.A., ~~Schut~~, G.J., ~~Nguyen, D~~.M., ~~Artz, J~~.H.~~, Tokmina~~-~~Lukaszewska~~, M., ~~Lipscomb~~, G.~~, Adams, M~~.W., ~~Peters, J~~.W.		== Structural highlights ==
			<table><tr><td colspan='2'>[[5jca]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JCA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5JCA FirstGlance]. <br>
	~~Description~~: NADP(H) ~~bound NADH~~-dependent ~~Ferredoxin~~:NADP ~~Oxidoreductase~~ (~~NfnI~~) ~~from Pyrococcus furiosus~~		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr>
	[[Category: ~~Unreleased Structures~~]]		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/NAD(P)(+)_transhydrogenase_(ferredoxin) NAD(P)(+) transhydrogenase (ferredoxin)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.6.1.4 1.6.1.4] </span></td></tr>
	[[Category: ~~Nguyen~~, D.M]]		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5jca FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jca OCA], [http://pdbe.org/5jca PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5jca RCSB], [http://www.ebi.ac.uk/pdbsum/5jca PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5jca ProSAT]</span></td></tr>
	[[Category: ~~Schut~~, G.J]]		</table>
			== Function ==
			[[http://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] [[http://www.uniprot.org/uniprot/SUDHB_PYRFU SUDHB_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> <ref>PMID:7961401</ref>
			== References ==
			<references/>
			__TOC__
			</StructureSection>
			[[Category: Pyrococcus furiosus]]
			[[Category: Adams, M W]]
			[[Category: Artz, J H]]
	[[Category: Lipscomb, G]]		[[Category: Lipscomb, G]]
	[[Category: ~~Adams~~, M.W]]		[[Category: Nguyen, D M]]
	[[Category: Peters, J.W]]		[[Category: Peters, J W]]
	[[Category: ~~Zadvornyy, O.A]]~~		[[Category: Schut, G J]]
	~~[[Category: Artz~~, J.H]]
	[[Category: Tokmina-Lukaszewska, M]]		[[Category: Tokmina-Lukaszewska, M]]
			[[Category: Zadvornyy, O A]]
			[[Category: Nfni]]
			[[Category: Oxidoreductase]]

OCA at 09:51, 9 March 2017

2017-03-09T09:51:01Z

← Older revision		Revision as of 09:51, 9 March 2017
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	Description: NADP(H) bound NADH-dependent Ferredoxin:NADP Oxidoreductase (NfnI) from Pyrococcus furiosus		Description: NADP(H) bound NADH-dependent Ferredoxin:NADP Oxidoreductase (NfnI) from Pyrococcus furiosus
	[[Category: Unreleased Structures]]		[[Category: Unreleased Structures]]
	~~[[Category: Adams, M.W]]~~
	~~[[Category: Peters, J.W]]~~
	~~[[Category: Artz, J.H]]~~
	[[Category: Nguyen, D.M]]		[[Category: Nguyen, D.M]]
	[[Category: Schut, G.J]]		[[Category: Schut, G.J]]
	[[Category: Lipscomb, G]]		[[Category: Lipscomb, G]]
			[[Category: Adams, M.W]]
			[[Category: Peters, J.W]]
	[[Category: Zadvornyy, O.A]]		[[Category: Zadvornyy, O.A]]
			[[Category: Artz, J.H]]
	[[Category: Tokmina-Lukaszewska, M]]		[[Category: Tokmina-Lukaszewska, M]]

OCA at 12:38, 20 June 2016

2016-06-20T12:38:38Z

← Older revision		Revision as of 12:38, 20 June 2016
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	'''Unreleased structure'''		'''Unreleased structure'''

	The entry 5jca is ON HOLD		The entry 5jca is ON HOLD until Paper Publication

	Authors: Zadvornyy, O.A., Schut, G.J., Nguyen, D.M., Artz, J.H., Tokmina-Lukaszewska, M., Lipscomb, G., Adams, M.W., Peters, J.W.		Authors: Zadvornyy, O.A., Schut, G.J., Nguyen, D.M., Artz, J.H., Tokmina-Lukaszewska, M., Lipscomb, G., Adams, M.W., Peters, J.W.

OCA at 13:17, 1 June 2016

2016-06-01T13:17:59Z

← Older revision		Revision as of 13:17, 1 June 2016
Line 3:		Line 3:
	The entry 5jca is ON HOLD		The entry 5jca is ON HOLD

	Authors: Zadvornyy, O.A., Artz, J. H, Peters, J.W.		Authors: Zadvornyy, O.A., Schut, G.J., Nguyen, D.M., Artz, J.H., Tokmina-Lukaszewska, M., Lipscomb, G., Adams, M.W., Peters, J.W.

	Description: NADP(H) bound NADH-dependent Ferredoxin:NADP Oxidoreductase (NfnI) from Pyrococcus furiosus		Description: NADP(H) bound NADH-dependent Ferredoxin:NADP Oxidoreductase (NfnI) from Pyrococcus furiosus
	[[Category: Unreleased Structures]]		[[Category: Unreleased Structures]]
	[[Category: Artz, J. H, ~~Peters~~, J.W]]		[[Category: Adams, M.W]]
			[[Category: Peters, J.W]]
			[[Category: Artz, J.H]]
			[[Category: Nguyen, D.M]]
			[[Category: Schut, G.J]]
			[[Category: Lipscomb, G]]
	[[Category: Zadvornyy, O.A]]		[[Category: Zadvornyy, O.A]]
			[[Category: Tokmina-Lukaszewska, M]]

OCA: Protected "5jca" [edit=sysop:move=sysop]

2016-05-11T01:50:30Z

Protected "5jca" [edit=sysop:move=sysop]

← Older revision	Revision as of 01:50, 11 May 2016
(No difference)