5xtd - Revision history

OCA at 08:54, 9 April 2025

2025-04-09T08:54:14Z

OCA at 22:37, 10 April 2020

2020-04-10T22:37:08Z

← Older revision		Revision as of 22:37, 10 April 2020
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	<SX load='5xtd' size='340' side='right' viewer='molstar' caption='[[5xtd]], [[Resolution\|resolution]] 3.70Å' scene=''>		<SX load='5xtd' size='340' side='right' viewer='molstar' caption='[[5xtd]], [[Resolution\|resolution]] 3.70Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[5xtd]] is a 45 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XTD OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5XTD FirstGlance]. <br>		<table><tr><td colspan='2'>[[5xtd]] is a 45 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XTD OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5XTD FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=8Q1:S-[2-({N-[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-beta-alanyl}amino)ethyl]+dodecanethioate'>8Q1</scene>, <scene name='pdbligand=CDL:CARDIOLIPIN'>CDL</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene>, <scene name='pdbligand=PEE:1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOETHANOLAMINE'>PEE</scene>, <scene name='pdbligand=PLX:(9R,11S)-9-({[(1S)-1-HYDROXYHEXADECYL]OXY}METHYL)-2,2-DIMETHYL-5,7,10-TRIOXA-2LAMBDA~5~-AZA-6LAMBDA~5~-PHOSPHAOCTACOSANE-6,6,11-TRIOL'>PLX</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=8Q1:S-[2-({N-[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-beta-alanyl}amino)ethyl]+dodecanethioate'>8Q1</scene>, <scene name='pdbligand=CDL:CARDIOLIPIN'>CDL</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene>, <scene name='pdbligand=PEE:1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOETHANOLAMINE'>PEE</scene>, <scene name='pdbligand=PLX:(9R,11S)-9-({[(1S)-1-HYDROXYHEXADECYL]OXY}METHYL)-2,2-DIMETHYL-5,7,10-TRIOXA-2LAMBDA~5~-AZA-6LAMBDA~5~-PHOSPHAOCTACOSANE-6,6,11-TRIOL'>PLX</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/NADH:ubiquinone_reductase_(H(+)-translocating) NADH:ubiquinone reductase (H(+)-translocating)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.6.5.3 1.6.5.3] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/NADH:ubiquinone_reductase_(H(+)-translocating) NADH:ubiquinone reductase (H(+)-translocating)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.6.5.3 1.6.5.3] </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=5xtd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xtd OCA], [http://pdbe.org/5xtd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5xtd RCSB], [http://www.ebi.ac.uk/pdbsum/5xtd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5xtd 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=5xtd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xtd OCA], [http://pdbe.org/5xtd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5xtd RCSB], [http://www.ebi.ac.uk/pdbsum/5xtd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5xtd ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==

OCA at 20:11, 6 March 2020

2020-03-06T20:11:22Z

Show changes

OCA at 07:27, 6 November 2019

2019-11-06T07:27:28Z

← Older revision		Revision as of 07:27, 6 November 2019
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	==Cryo-EM structure of human respiratory complex I==		==Cryo-EM structure of human respiratory complex I==
	<StructureSection load='5xtd' size='340' side='right' caption='[[5xtd]], [[Resolution\|resolution]] 3.70Å' scene=''>		<StructureSection load='5xtd' size='340' side='right'caption='[[5xtd]], [[Resolution\|resolution]] 3.70Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[5xtd]] is a 45 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XTD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5XTD FirstGlance]. <br>		<table><tr><td colspan='2'>[[5xtd]] is a 45 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XTD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5XTD FirstGlance]. <br>
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	</StructureSection>		</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
			[[Category: Large Structures]]
	[[Category: Gu, J]]		[[Category: Gu, J]]
	[[Category: Wu, M]]		[[Category: Wu, M]]

OCA at 07:57, 6 December 2017

2017-12-06T07:57:04Z

Show changes

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

2017-09-05T15:07:39Z

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

← Older revision	Revision as of 15:07, 5 September 2017
(No difference)

OCA: New page: ==Cryo-EM structure of human respiratory complex I== == Structura...

2017-09-05T15:07:37Z

New page: ==Cryo-EM structure of human respiratory complex I== <StructureSection load='5xtd' size='340' side='right' caption='5xtd, resolution 3.70Å' scene=''> == Structura...

New page

==Cryo-EM structure of human respiratory complex I==
<StructureSection load='5xtd' size='340' side='right' caption='[[5xtd]], [[Resolution|resolution]] 3.70Å' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5xtd]] is a 45 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XTD OCA]. For a guided tour on the structure components use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5XTD FirstGlance]. 
</td></tr><tr id='ligand'><td class="sblockLbl">[[Ligand|Ligands:]]</td><td class="sblockDat"><scene name='pdbligand=8Q1:S-[2-({N-[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-beta-alanyl}amino)ethyl]+dodecanethioate'>8Q1</scene>, <scene name='pdbligand=CDL:CARDIOLIPIN'>CDL</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene>, <scene name='pdbligand=PEE:1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOETHANOLAMINE'>PEE</scene>, <scene name='pdbligand=PLX:(9R,11S)-9-({[(1S)-1-HYDROXYHEXADECYL]OXY}METHYL)-2,2-DIMETHYL-5,7,10-TRIOXA-2LAMBDA~5~-AZA-6LAMBDA~5~-PHOSPHAOCTACOSANE-6,6,11-TRIOL'>PLX</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr>
<tr id='activity'><td class="sblockLbl">Activity:</td><td class="sblockDat">[http://en.wikipedia.org/wiki/NADH:ubiquinone_reductase_(H(+)-translocating) NADH:ubiquinone reductase (H(+)-translocating)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.6.5.3 1.6.5.3] </td></tr>
<tr id='resources'><td class="sblockLbl">Resources:</td><td class="sblockDat">[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5xtd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xtd OCA], [http://pdbe.org/5xtd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5xtd RCSB], [http://www.ebi.ac.uk/pdbsum/5xtd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5xtd ProSAT]</td></tr>
</table>
== Disease ==
[[http://www.uniprot.org/uniprot/NDUAD_HUMAN NDUAD_HUMAN]] Papillary or follicular thyroid carcinoma. Disease susceptibility is associated with variations affecting the gene represented in this entry. Defects in NDUFA13 are a cause of a mitochondrial complex I deficiency characterized by early onset hypotonia, dyskinesia and sensorial deficiencies, as well as a severe optic neuropathy.<ref>PMID:25901006</ref> [[http://www.uniprot.org/uniprot/NDUA1_HUMAN NDUA1_HUMAN]] Isolated NADH-CoQ reductase deficiency. The disease is caused by mutations affecting the gene represented in this entry. [[http://www.uniprot.org/uniprot/NDUS8_HUMAN NDUS8_HUMAN]] Isolated NADH-CoQ reductase deficiency;Leigh syndrome with leukodystrophy. The disease is caused by mutations affecting the gene represented in this entry. [[http://www.uniprot.org/uniprot/NDUV1_HUMAN NDUV1_HUMAN]] Isolated NADH-CoQ reductase deficiency;Leigh syndrome with leukodystrophy. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. [[http://www.uniprot.org/uniprot/NDUS6_HUMAN NDUS6_HUMAN]] Isolated NADH-CoQ reductase deficiency. The disease is caused by mutations affecting the gene represented in this entry. [[http://www.uniprot.org/uniprot/NDUAA_HUMAN NDUAA_HUMAN]] Leigh syndrome with leukodystrophy. The disease is caused by mutations affecting the gene represented in this entry. [[http://www.uniprot.org/uniprot/NDUBB_HUMAN NDUBB_HUMAN]] The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. The disease may be caused by mutations affecting the gene represented in this entry. [[http://www.uniprot.org/uniprot/NDUAB_HUMAN NDUAB_HUMAN]] Isolated NADH-CoQ reductase deficiency. The disease is caused by mutations affecting the gene represented in this entry. [[http://www.uniprot.org/uniprot/NDUV2_HUMAN NDUV2_HUMAN]] Isolated NADH-CoQ reductase deficiency. [[http://www.uniprot.org/uniprot/NDUS4_HUMAN NDUS4_HUMAN]] Isolated NADH-CoQ reductase deficiency;Leigh syndrome with leukodystrophy. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. [[http://www.uniprot.org/uniprot/NDUAC_HUMAN NDUAC_HUMAN]] The disease is caused by mutations affecting the gene represented in this entry. [[http://www.uniprot.org/uniprot/NDUB3_HUMAN NDUB3_HUMAN]] Isolated NADH-CoQ reductase deficiency. The disease is caused by mutations affecting the gene represented in this entry. [[http://www.uniprot.org/uniprot/NDUB9_HUMAN NDUB9_HUMAN]] Isolated NADH-CoQ reductase deficiency. [[http://www.uniprot.org/uniprot/NDUS7_HUMAN NDUS7_HUMAN]] Isolated NADH-CoQ reductase deficiency;Leigh syndrome with leukodystrophy. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. [[http://www.uniprot.org/uniprot/NDUA9_HUMAN NDUA9_HUMAN]] Isolated NADH-CoQ reductase deficiency. The disease is caused by mutations affecting the gene represented in this entry. [[http://www.uniprot.org/uniprot/NDUS1_HUMAN NDUS1_HUMAN]] Isolated NADH-CoQ reductase deficiency;Leigh syndrome with leukodystrophy. The disease is caused by mutations affecting the gene represented in this entry. [[http://www.uniprot.org/uniprot/NDUS3_HUMAN NDUS3_HUMAN]] Isolated NADH-CoQ reductase deficiency;Leigh syndrome with leukodystrophy.
== Function ==
[[http://www.uniprot.org/uniprot/B9EE38_HUMAN B9EE38_HUMAN]] Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.[SAAS:SAAS00136983] [[http://www.uniprot.org/uniprot/Q4GRX1_HUMAN Q4GRX1_HUMAN]] Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.[SAAS:SAAS00093760] [[http://www.uniprot.org/uniprot/NDUAD_HUMAN NDUAD_HUMAN]] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis (PubMed:27626371). Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (PubMed:27626371). Involved in the interferon/all-trans-retinoic acid (IFN/RA) induced cell death. This apoptotic activity is inhibited by interaction with viral IRF1. Prevents the transactivation of STAT3 target genes. May play a role in CARD15-mediated innate mucosal responses and serve to regulate intestinal epithelial cell responses to microbes (PubMed:15753091).<ref>PMID:12628925</ref> <ref>PMID:12867595</ref> <ref>PMID:15753091</ref> <ref>PMID:27626371</ref> [[http://www.uniprot.org/uniprot/NDUA5_HUMAN NDUA5_HUMAN]] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.<ref>PMID:27626371</ref> [[http://www.uniprot.org/uniprot/NDUB8_HUMAN NDUB8_HUMAN]] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.<ref>PMID:27626371</ref> [[http://www.uniprot.org/uniprot/NDUA1_HUMAN NDUA1_HUMAN]] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.<ref>PMID:27626371</ref> [[http://www.uniprot.org/uniprot/NDUS8_HUMAN NDUS8_HUMAN]] Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity). May donate electrons to ubiquinone. [[http://www.uniprot.org/uniprot/NDUV1_HUMAN NDUV1_HUMAN]] Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity). [[http://www.uniprot.org/uniprot/NDUS6_HUMAN NDUS6_HUMAN]] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.<ref>PMID:27626371</ref> [[http://www.uniprot.org/uniprot/NDUC2_HUMAN NDUC2_HUMAN]] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.<ref>PMID:27626371</ref> [[http://www.uniprot.org/uniprot/NDUAA_HUMAN NDUAA_HUMAN]] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.<ref>PMID:27626371</ref> [[http://www.uniprot.org/uniprot/NDUBA_HUMAN NDUBA_HUMAN]] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.<ref>PMID:27626371</ref> [[http://www.uniprot.org/uniprot/NDUB6_HUMAN NDUB6_HUMAN]] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.<ref>PMID:27626371</ref> [[http://www.uniprot.org/uniprot/NDUBB_HUMAN NDUBB_HUMAN]] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.<ref>PMID:27626371</ref> [[http://www.uniprot.org/uniprot/NDUAB_HUMAN NDUAB_HUMAN]] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.<ref>PMID:27626371</ref> [[http://www.uniprot.org/uniprot/NDUV2_HUMAN NDUV2_HUMAN]] Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity). [[http://www.uniprot.org/uniprot/NDUB5_HUMAN NDUB5_HUMAN]] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.<ref>PMID:27626371</ref> [[http://www.uniprot.org/uniprot/NDUV3_HUMAN NDUV3_HUMAN]] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. May be the terminally assembled subunit of Complex I.<ref>PMID:27626371</ref> [[http://www.uniprot.org/uniprot/NDUS5_HUMAN NDUS5_HUMAN]] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.<ref>PMID:27626371</ref> [[http://www.uniprot.org/uniprot/X5BVZ3_HUMAN X5BVZ3_HUMAN]] Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.[SAAS:SAAS00061107] [[http://www.uniprot.org/uniprot/NDUS4_HUMAN NDUS4_HUMAN]] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.<ref>PMID:12611891</ref> <ref>PMID:9463323</ref> [[http://www.uniprot.org/uniprot/NDUB2_HUMAN NDUB2_HUMAN]] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.<ref>PMID:27626371</ref> [[http://www.uniprot.org/uniprot/NDUAC_HUMAN NDUAC_HUMAN]] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.<ref>PMID:27626371</ref> [[http://www.uniprot.org/uniprot/NDUB3_HUMAN NDUB3_HUMAN]] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.<ref>PMID:27626371</ref> [[http://www.uniprot.org/uniprot/NDUC1_HUMAN NDUC1_HUMAN]] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.<ref>PMID:27626371</ref> [[http://www.uniprot.org/uniprot/ACPM_HUMAN ACPM_HUMAN]] Carrier of the growing fatty acid chain in fatty acid biosynthesis in mitochondria. Accessory and non-catalytic subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), which functions in the transfer of electrons from NADH to the respiratory chain (By similarity). [[http://www.uniprot.org/uniprot/NDUB9_HUMAN NDUB9_HUMAN]] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed to be not involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.<ref>PMID:27626371</ref> [[http://www.uniprot.org/uniprot/NDUS7_HUMAN NDUS7_HUMAN]] Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.<ref>PMID:12611891</ref> [[http://www.uniprot.org/uniprot/NDUA9_HUMAN NDUA9_HUMAN]] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.<ref>PMID:22114105</ref> <ref>PMID:27626371</ref> [[http://www.uniprot.org/uniprot/NDUS1_HUMAN NDUS1_HUMAN]] Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity). This is the largest subunit of complex I and it is a component of the iron-sulfur (IP) fragment of the enzyme. It may form part of the active site crevice where NADH is oxidized. [[http://www.uniprot.org/uniprot/NDUS3_HUMAN NDUS3_HUMAN]] Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity). [[http://www.uniprot.org/uniprot/NDUB4_HUMAN NDUB4_HUMAN]] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.<ref>PMID:27626371</ref> [[http://www.uniprot.org/uniprot/NDUA7_HUMAN NDUA7_HUMAN]] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.<ref>PMID:27626371</ref> [[http://www.uniprot.org/uniprot/NDUA6_HUMAN NDUA6_HUMAN]] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed to be not involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.<ref>PMID:27626371</ref> [[http://www.uniprot.org/uniprot/V9JN72_HUMAN V9JN72_HUMAN]] Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.[RuleBase:RU004419] [[http://www.uniprot.org/uniprot/NDUB1_HUMAN NDUB1_HUMAN]] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.<ref>PMID:27626371</ref> [[http://www.uniprot.org/uniprot/NDUB7_HUMAN NDUB7_HUMAN]] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.<ref>PMID:27626371</ref> [[http://www.uniprot.org/uniprot/NDUA3_HUMAN NDUA3_HUMAN]] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.<ref>PMID:27626371</ref> [[http://www.uniprot.org/uniprot/NDUA2_HUMAN NDUA2_HUMAN]] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Gu, J]]
[[Category: Wu, M]]
[[Category: Yang, M]]
[[Category: Homo sapien]]
[[Category: Oxidoreductase]]
[[Category: Oxidoreductase-electron transport complex]]
[[Category: Respiratory]]