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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 chemistry genetics enzymology 
Crystallography, X-Ray Humans Amino Acid Sequence Hydrogen Bonding Models, Molecular Molecular Sequence Data Catalysis Protein Conformation Protein Structure, Quaternary Static Electricity Sequence Homology, Amino Acid Recombinant Proteins Kinetics Substrate Specificity Indoleamine-Pyrrole 2,3,-Dioxygenase Xanthomonas campestris Allosteric Site Shewanella Tryptophan Oxygenase 
17197414  
10.1073/pnas.0610007104  
121 (Last update: 11/17/2018 12:06:31pm)  
2NWB
2NW7
2NW8
2NW9  
structure  
multiple pdbids [2nwb,1yw0, 1zee,2nw7 ]