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1FS5

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

Summary for 1FS5
Entry DOI10.2210/pdb1fs5/pdb
Related1CD5 1D9T 1DEA 1FQO 1FRZ 1HOR 1HOT
DescriptorGLUCOSAMINE-6-PHOSPHATE DEAMINASE, 2-acetamido-2-deoxy-6-O-phosphono-alpha-D-glucopyranose, L(+)-TARTARIC ACID, ... (4 entities in total)
Functional Keywordsallosteric enzyme, entropic effects, aldose-ketose isomerase, multiple conformers, isomerase
Biological sourceEscherichia coli
Total number of polymer chains2
Total formula weight60376.88
Authors
Rudino-Pinera, E.,Morales-Arrieta, S.,Rojas-Trejo, S.P.,Horjales, E. (deposition date: 2000-09-08, release date: 2002-01-04, Last modification date: 2024-02-07)
Primary citationRudino-Pinera, E.,Morales-Arrieta, S.,Rojas-Trejo, S.P.,Horjales, E.
Structural flexibility, an essential component of the allosteric activation in Escherichia coli glucosamine-6-phosphate deaminase.
Acta Crystallogr.,Sect.D, 58:10-20, 2002
Cited by
PubMed: 11752775
DOI: 10.1107/S0907444901016699
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.73 Å)
Structure validation

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