2.6.1.16	molecular dynamics simulations. Key role for Trp74, in the sealing of the hydrophobic channel connecting the two binding sites, as well as for the two Ala602 and Val605 residues, which form a narrow passage whose opening/closing constitutes an essential event in ammonia transfer	673687	
2.6.1.16	molecular model of the 3-D on the basis of the crystal structures of Escherichia coli GlcN-6-P synthase, PDB entry 4AMV and Candida albicans GlcN-6-P synthase, PDB entry 2POC. The protein has a terminal glutamine amidotransferase type 2 domain (residues 2-318). The phosphosugar-binding SIS domain (residues 390-529; 562-707) plays a key role in catalysis and communication of fructose 6-phosphate and D-glucosamine 6-phosphate between the two active sites	737920	
2.6.1.16	the crystal structure of the C1A mutant of Escherichia coli GlmS, solved at 2.5 A resolution, is organized as a hexamer, where the glutaminase domains adopt an inactive conformation	722779	
2.6.1.16	two crystal complexes of the isomerase domain with D-glucose 6-phosphate and 2-amino-2-deoxyglucitol 6-phosphate	639930