A DISCOVERY OF THREE ALTERNATE CONFORMATIONS IN THE ACTIVE SITE OF GLUCOSAMINE-6-PHOSPHATE ISOMERASE

A DISCOVERY OF THREE ALTERNATE CONFORMATIONS IN THE ACTIVE SITE OF GLUCOSAMINE-6-PHOSPHATE ISOMERASE Descriptor: 2-acetamido-2-deoxy-6-O-phosphono-alpha-D-glucopyranose, GLUCOSAMINE-6-PHOSPHATE DEAMINASE, L(+)-TARTARIC ACID Authors: Rudino-Pinera, E, Morales-Arrieta, S, Rojas-Trejo, S.P, Horjales, E. Deposit date: 2000-09-08 Release date: 2002-01-04 Last modified: 2024-02-07 Method: X-RAY DIFFRACTION (1.73 Å) Cite: Structural flexibility, an essential component of the allosteric activation in Escherichia coli glucosamine-6-phosphate deaminase. Acta Crystallogr.,Sect.D, 58, 2002