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Molecular insights into substrate recognition and catalysis by tryptophan 2,3-dioxygenase.

Forouhar F, Anderson JL, Mowat CG, Vorobiev SM, Hussain A, Abashidze M, Bruckmann C, Thackray SJ, Seetharaman J, Tucker T, Xiao R, Ma LC, Zhao L, Acton TB, Montelione GT, Chapman SK, Tong L,
Proceedings of the National Academy of Sciences of the United States of America (2007) 104(2):473-8 PublishedPSI:Phase 2  
Northeast Structural Genomics Consortium

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Tryptophan 2,3-dioxygenase (TDO) and indoleamine 2,3-dioxygenase (IDO) constitute an important, yet relatively poorly understood, family of heme-containing enzymes. ...
metabolism enzymology chemistry genetics 
Crystallography, X-Ray Shewanella Protein Conformation Substrate Specificity Indoleamine-Pyrrole 2,3,-Dioxygenase Amino Acid Sequence Sequence Homology, Amino Acid Hydrogen Bonding Models, Molecular Recombinant Proteins Protein Structure, Quaternary Humans Xanthomonas campestris Molecular Sequence Data Allosteric Site Tryptophan Oxygenase Kinetics Catalysis Static Electricity 
17197414  
10.1073/pnas.0610007104  
114 (Last update: 07/15/2017 11:12:26am)  
2NWB
2NW7
2NW8
2NW9  
structure  
multiple pdbids [2nwb,1yw0, 1zee,2nw7 ]