1CD5

GLUCOSAMINE-6-PHOSPHATE DEAMINASE FROM E.COLI, T CONFORMER

Summary for 1CD5

Entry DOI	10.2210/pdb1cd5/pdb
Descriptor	PROTEIN (GLUCOSAMINE 6-PHOSPHATE DEAMINASE) (2 entities in total)
Functional Keywords	allosteric enzyme, entropic effects, aldose-ketose isomerase, isomerase
Biological source	Escherichia coli
Total number of polymer chains	1
Total formula weight	29812.21
Authors	Horjales, E.,Altamirano, M.M.,Calcagno, M.L.,Garratt, R.C.,Oliva, G. (deposition date: 1999-03-05, release date: 2000-03-06, Last modification date: 2023-08-09)
Primary citation	Horjales, E.,Altamirano, M.M.,Calcagno, M.L.,Garratt, R.C.,Oliva, G. The allosteric transition of glucosamine-6-phosphate deaminase: the structure of the T state at 2.3 A resolution. Structure Fold.Des., 7:527-537, 1999 Cited by PubMed Abstract: The allosteric hexameric enzyme glucosamine-6-phosphate deaminase from Escherichia coli catalyses the regulatory step of N-acetylglucosamine catabolism, which consists of the isomerisation and deamination of glucosamine 6-phosphate (GlcN6P) to form fructose 6-phosphate (Fru6P) and ammonia. The reversibility of the catalysis and its rapid-equilibrium random kinetic mechanism, among other properties, make this enzyme a good model for studying allosteric processes. PubMed: 10378272 DOI: 10.1016/S0969-2126(99)80069-0 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.3 Å)

Structure validation