1s3a

<StructureSection load='1s3a' size='340' side='right'caption='[[1s3a]], [[NMR_Ensembles_of_Models | 19 NMR models]]' scene=''>

<table><tr><td colspan='2'>[[1s3a]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S3A OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1S3A FirstGlance]. <br>

</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">NDUFA2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=1s3a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s3a OCA], [http://pdbe.org/1s3a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1s3a RCSB], [http://www.ebi.ac.uk/pdbsum/1s3a PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1s3a ProSAT]</span></td></tr>

[[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.

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

Subunit B8 from ubiquinone oxidoreductase (complex I) (CI-B8) is one of several nuclear-encoded supernumerary subunits that are not present in bacterial complex I. Its solution structure shows a thioredoxin fold with highest similarities to the human thioredoxin mutant C73S and thioredoxin 2 from Anabeana sp. Interestingly, these proteins contain active sites in the same area, where the disulfide bond of oxidized CI-B8 is located. The redox potential of this disulfide bond is -251.6 mV, comparing well to that of disulfides in other thioredoxin-like proteins. Analysis of the structure reveals a surface area that is exclusively composed of highly conserved residues and thus most likely a subunit interaction site within complex I.

The oxidized subunit B8 from human complex I adopts a thioredoxin fold.,Brockmann C, Diehl A, Rehbein K, Strauss H, Schmieder P, Korn B, Kuhne R, Oschkinat H Structure. 2004 Sep;12(9):1645-54. PMID:15341729<ref>PMID:15341729</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

</div>

<div class="pdbe-citations 1s3a" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Human]]

[[Category: Brockmann, C]]

[[Category: Diehl, A]]

[[Category: Kuhne, R]]

[[Category: Oschkinat, H]]

[[Category: Rehbein, K]]

[[Category: Oxidoreductase]]