Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004347 | molecular_function | glucose-6-phosphate isomerase activity |
A | 0005125 | molecular_function | cytokine activity |
A | 0005576 | cellular_component | extracellular region |
A | 0005615 | cellular_component | extracellular space |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0006094 | biological_process | gluconeogenesis |
A | 0006096 | biological_process | glycolytic process |
A | 0007165 | biological_process | signal transduction |
A | 0016853 | molecular_function | isomerase activity |
A | 0048029 | molecular_function | monosaccharide binding |
A | 0051156 | biological_process | glucose 6-phosphate metabolic process |
A | 0097367 | molecular_function | carbohydrate derivative binding |
A | 1901135 | biological_process | carbohydrate derivative metabolic process |
B | 0004347 | molecular_function | glucose-6-phosphate isomerase activity |
B | 0005125 | molecular_function | cytokine activity |
B | 0005576 | cellular_component | extracellular region |
B | 0005615 | cellular_component | extracellular space |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0006094 | biological_process | gluconeogenesis |
B | 0006096 | biological_process | glycolytic process |
B | 0007165 | biological_process | signal transduction |
B | 0016853 | molecular_function | isomerase activity |
B | 0048029 | molecular_function | monosaccharide binding |
B | 0051156 | biological_process | glucose 6-phosphate metabolic process |
B | 0097367 | molecular_function | carbohydrate derivative binding |
B | 1901135 | biological_process | carbohydrate derivative metabolic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE S6P A 2002 |
Chain | Residue |
A | GLY157 |
A | GLN353 |
A | GLU357 |
A | GLN511 |
A | HOH3067 |
A | HOH3129 |
A | HOH3215 |
A | HOH3247 |
A | HOH3328 |
B | HIS1388 |
A | GLY158 |
A | SER159 |
A | SER209 |
A | LYS210 |
A | THR211 |
A | THR214 |
A | GLY271 |
A | ARG272 |
site_id | AC2 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE S6P B 2001 |
Chain | Residue |
A | HIS388 |
B | GLY1157 |
B | GLY1158 |
B | SER1159 |
B | SER1209 |
B | LYS1210 |
B | THR1211 |
B | THR1214 |
B | GLY1271 |
B | ARG1272 |
B | GLN1353 |
B | GLU1357 |
B | HOH3126 |
B | HOH3165 |
B | HOH3182 |
B | HOH3194 |
B | HOH3244 |
B | HOH3268 |
B | HOH3305 |
Functional Information from PROSITE/UniProt
site_id | PS00174 |
Number of Residues | 18 |
Details | P_GLUCOSE_ISOMERASE_2 Phosphoglucose isomerase signature 2. GvVWdinsFDQwGVElgK |
Chain | Residue | Details |
A | GLY501-LYS518 | |
site_id | PS00765 |
Number of Residues | 14 |
Details | P_GLUCOSE_ISOMERASE_1 Phosphoglucose isomerase signature 1. DwVGGRYSLwSAIG |
Chain | Residue | Details |
A | ASP267-GLY280 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | GLU357 | |
B | GLU1357 | |
Chain | Residue | Details |
A | HIS388 | |
A | LYS518 | |
B | HIS1388 | |
B | LYS1518 | |
Chain | Residue | Details |
A | GLY158 | |
B | HIS1388 | |
A | SER209 | |
A | GLN353 | |
A | GLU357 | |
A | HIS388 | |
B | GLY1158 | |
B | SER1209 | |
B | GLN1353 | |
B | GLU1357 | |
Chain | Residue | Details |
A | LYS518 | |
B | LYS1518 | |
Chain | Residue | Details |
A | ALA1 | |
B | ALA1001 | |
Chain | Residue | Details |
A | LYS11 | |
A | LYS141 | |
B | LYS1011 | |
B | LYS1141 | |
Chain | Residue | Details |
A | LYS33 | |
B | LYS1033 | |
Chain | Residue | Details |
A | SER106 | |
A | SER454 | |
B | SER1106 | |
B | SER1454 | |
Chain | Residue | Details |
A | THR108 | |
B | THR1108 | |
Chain | Residue | Details |
A | SER184 | |
B | SER1184 | |
Chain | Residue | Details |
A | THR249 | |
B | THR1249 | |
Chain | Residue | Details |
A | LYS453 | |
B | LYS1453 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 7 |
Details | Annotated By Reference To The Literature 1dqr |
Chain | Residue | Details |
A | HIS388 | |
B | GLY1271 | |
B | LYS1518 | |
B | LYS1210 | |
B | GLU1216 | |
B | GLU1357 | |
B | ARG1272 | |
site_id | CSA2 |
Number of Residues | 7 |
Details | Annotated By Reference To The Literature 1dqr |
Chain | Residue | Details |
A | ARG272 | |
A | LYS518 | |
A | GLU216 | |
A | GLU357 | |
A | LYS210 | |
A | GLY271 | |
B | HIS1388 | |
site_id | MCSA1 |
Number of Residues | 7 |
Details | M-CSA 842 |
Chain | Residue | Details |
A | LYS210 | electrostatic stabiliser |
A | GLU216 | modifies pKa |
A | GLY271 | electrostatic stabiliser |
A | ARG272 | electrostatic stabiliser |
A | GLU357 | proton acceptor, proton donor |
A | HIS388 | proton acceptor, proton donor |
A | LYS518 | proton acceptor, proton donor |
site_id | MCSA2 |
Number of Residues | 7 |
Details | M-CSA 842 |
Chain | Residue | Details |
B | LYS1210 | electrostatic stabiliser |
B | GLU1216 | modifies pKa |
B | GLY1271 | electrostatic stabiliser |
B | ARG1272 | electrostatic stabiliser |
B | GLU1357 | proton acceptor, proton donor |
B | HIS1388 | proton acceptor, proton donor |
B | LYS1518 | proton acceptor, proton donor |