2j3n
From Proteopedia
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X-RAY STRUCTURE OF HUMAN THIOREDOXIN REDUCTASE 1
Overview
Human thioredoxin reductase (hTrxR) is a homodimeric flavoprotein, crucially involved in the regulation of cellular redox reactions, growth, and differentiation. The enzyme contains a selenocysteine residue at its, C-terminal active site that is essential for catalysis. This redox center, is located on a flexible arm, solvent-exposed and reactive towards, electrophilic inhibitors, thus representing a target for antitumor drug, development. During catalysis reducing equivalents are transferred from, the cofactor NADPH to FAD, then to the N-terminal active site cysteine, residues and from there to the flexible C-terminal part of the other, subunit to be finally delivered to a variety of second substrates at the, molecule's surface. Here we report the first crystal structure of hTrxR1, ... [(full description)]
About this Structure
2J3N is a [Single protein] structure of sequence from [Homo sapiens] with FAD, NAP and MPD as [ligands]. Active as [[1]], with EC number [1.8.1.9]. Full crystallographic information is available from [OCA].
Reference
The structure of human thioredoxin reductase 1 provides insights into C-terminal rearrangements during catalysis., Fritz-Wolf K, Urig S, Becker K, J Mol Biol. 2007 Jun 29;370(1):116-27. Epub 2007 Apr 24. PMID:17512005
Page seeded by OCA on Mon Oct 29 19:32:10 2007
Categories: Homo sapiens | Single protein | Becker, K. | Fritz-Wolf, K. | Urig, S. | FAD | MPD | NAP | Cytoplasm | Electron transport | Fad | Flavoprotein | Human | Nadp | Oxidoreductase | Phosphorylation | Pyridine nucleotide dependent disulfide reductase | Redox regulation | Redox-active center | Selenium | Selenocysteine