1.7.1.13	construction of homology model and docking studies of natural and non-natural substrates. Residues C190 and D197 play an essential role in the catalytic mechanism	724767	
1.7.1.13	hanging drop vapor diffusion method, using 0.04 M sodium dihydrogen phosphate, 0.96 M dipotassium hydrogen phosphate, and 10 mM GTP	712770	
1.7.1.13	homology model based on the crystal structure of nitrile reductase from Vibrio cholerae, PDB ID 3uxv. The side chain of residue Glu89 and the main chain of Ser90 form hydrogen bonds with the ring nitrogen atoms of the substrate. The carboxylate group of Glu230 also forms hydrogen bonds with the substrate preQ0. The aromatic ring of Phe228 may form a pi-pi-stacking interaction with the aromatic ring of preQ0, while the main chain of His229coordinates the keto-functionality of the substrate	743107	
1.7.1.13	sitting-drop vapor-diffusion method, space group: P3(1)21. Unit-cell parameters: a = b = 93.52 A, c = 193.76 A	660634	
1.7.1.13	structure of mutant E97Q, displays an intramolecular disulfide formed between the catalytic Cys55 and a conserved Cys99 located near the active site. This structure exhibits major rearrangement of the loops responsible for substrate binding	742061