2nvk

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Revision as of 07:05, 27 July 2012

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spinqualitylabelsall models PDB ID 2nvk Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image
2nvk, resolution 2.40Å ()
Ligands:	,
Gene:	Trxr-1 (Drosophila melanogaster)
Activity:	Thioredoxin-disulfide reductase, with EC number 1.8.1.9
Structural annotation: Resources: InterPro : Ipr001327, Ipr000815, Ipr012999, Ipr004099, Ipr013027, Ipr006338, Ipr001100 Pfam : PF02852, PF00070, PF07992 UniProt : P91938
Functional annotation: Cellular component: mitochondrion cytoplasm Biological process: thioredoxin pathway cell redox homeostasis electron transport determination of adult life span Molecular function: oxidoreductase activity, acting on NADH or NADPH, disulfide as acceptor thioredoxin-disulfide reductase activity FAD binding oxidoreductase activity antioxidant activity protein binding NADP binding glutathione-disulfide reductase activity
Evolutionary conservation: Toggle Conservation Colors: Rows = identical sequences: Further Information: Caveats, Explanation, Complete Results at ConSurfDB
Resources:	FirstGlance, OCA, RCSB, PDBsum
Coordinates:	save as pdb, mmCIF, xml

Contents 1 Crystal Structure of Thioredoxin Reductase from Drosophila melanogaster 2 About this Structure 3 See Also 4 Reference

Crystal Structure of Thioredoxin Reductase from Drosophila melanogaster

Template:ABSTRACT PUBMED 17385893

About this Structure

2nvk is a 1 chain structure of Thioredoxin Reductase with sequence from Drosophila melanogaster. Full crystallographic information is available from OCA.

See Also

• Thioredoxin Reductase
• User:Sarah Abdalla/Thioredoxin Reductase

Reference

• Eckenroth BE, Rould MA, Hondal RJ, Everse SJ. Structural and biochemical studies reveal differences in the catalytic mechanisms of mammalian and Drosophila melanogaster thioredoxin reductases. Biochemistry. 2007 Apr 24;46(16):4694-705. Epub 2007 Mar 27. PMID:17385893 doi:10.1021/bi602394p