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3PR3

Crystal structure of Plasmodium falciparum glucose-6-phosphate isomerase (PF14_0341) in complex with fructose-6-phosphate

Functional Information from GO Data
ChainGOidnamespacecontents
A0004347molecular_functionglucose-6-phosphate isomerase activity
A0005829cellular_componentcytosol
A0006094biological_processgluconeogenesis
A0006096biological_processglycolytic process
A0006098biological_processpentose-phosphate shunt
A0016853molecular_functionisomerase activity
A0048029molecular_functionmonosaccharide binding
A0051156biological_processglucose 6-phosphate metabolic process
A0097367molecular_functioncarbohydrate derivative binding
A1901135biological_processcarbohydrate derivative metabolic process
B0004347molecular_functionglucose-6-phosphate isomerase activity
B0005829cellular_componentcytosol
B0006094biological_processgluconeogenesis
B0006096biological_processglycolytic process
B0006098biological_processpentose-phosphate shunt
B0016853molecular_functionisomerase activity
B0048029molecular_functionmonosaccharide binding
B0051156biological_processglucose 6-phosphate metabolic process
B0097367molecular_functioncarbohydrate derivative binding
B1901135biological_processcarbohydrate derivative metabolic process
Functional Information from PROSITE/UniProt
site_idPS00174
Number of Residues18
DetailsP_GLUCOSE_ISOMERASE_2 Phosphoglucose isomerase signature 2. GfLLninsFDQwGVElgK
ChainResidueDetails
AGLY523-LYS540

site_idPS00765
Number of Residues14
DetailsP_GLUCOSE_ISOMERASE_1 Phosphoglucose isomerase signature 1. DwVGGRFSVtSSVG
ChainResidueDetails
AASP289-GLY302

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PDB entries from 2024-09-04

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