1NUH

The crystal structure of human phosphoglucose isomerase complexed with 5-phosphoarabinonate

Summary for 1NUH

Entry DOI	10.2210/pdb1nuh/pdb
Related	1IAT
Descriptor	glucose phosphate isomerase, SULFATE ION, 5-PHOSPHOARABINONIC ACID, ... (4 entities in total)
Functional Keywords	aldose-ketose isomerase, glycolysis enzyme, neurotrophic growth factor, cytokine, isomerase
Biological source	Homo sapiens (human)
Cellular location	Cytoplasm : P06744
Total number of polymer chains	1
Total formula weight	64052.44
Authors	Davies, C. (deposition date: 2003-01-31, release date: 2003-02-11, Last modification date: 2023-08-16)
Primary citation	Davies, C.,Muirhead, H.,Chirgwin, J. The structure of human phosphoglucose isomerase complexed with a transition-state analogue. Acta Crystallogr.,Sect.D, 59:1111-1113, 2003 Cited by PubMed Abstract: Phosphoglucose isomerase (PGI) is a workhorse enzyme of carbohydrate metabolism that interconverts glucose 6-phosphate and fructose 6-phosphate. Outside the cell, however, the protein appears to function as a cytokine. A crystal structure of human PGI bound with 5-phosphoarabinonate, a strong inhibitor that mimics the cis-enediol(ate) intermediate of the reaction, has been determined at 2.5 A resolution. The structure helps to confirm the assignment of Glu357 as the base catalyst in the isomerase reaction. PubMed: 12777791 DOI: 10.1107/S0907444903007352 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.51 Å)

Structure validation