2O2D
Crystal structure of phosphoglucose isomerase from Trypanosoma brucei complexed with citrate
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004347 | molecular_function | glucose-6-phosphate isomerase activity |
A | 0005777 | cellular_component | peroxisome |
A | 0005829 | cellular_component | cytosol |
A | 0006094 | biological_process | gluconeogenesis |
A | 0006096 | biological_process | glycolytic process |
A | 0016853 | molecular_function | isomerase activity |
A | 0020015 | cellular_component | glycosome |
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 | 0005777 | cellular_component | peroxisome |
B | 0005829 | cellular_component | cytosol |
B | 0006094 | biological_process | gluconeogenesis |
B | 0006096 | biological_process | glycolytic process |
B | 0016853 | molecular_function | isomerase activity |
B | 0020015 | cellular_component | glycosome |
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 |
C | 0004347 | molecular_function | glucose-6-phosphate isomerase activity |
C | 0005777 | cellular_component | peroxisome |
C | 0005829 | cellular_component | cytosol |
C | 0006094 | biological_process | gluconeogenesis |
C | 0006096 | biological_process | glycolytic process |
C | 0016853 | molecular_function | isomerase activity |
C | 0020015 | cellular_component | glycosome |
C | 0048029 | molecular_function | monosaccharide binding |
C | 0051156 | biological_process | glucose 6-phosphate metabolic process |
C | 0097367 | molecular_function | carbohydrate derivative binding |
C | 1901135 | biological_process | carbohydrate derivative metabolic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE CIT A 5001 |
Chain | Residue |
A | ILE205 |
A | HIS442 |
A | HOH7059 |
A | HOH7234 |
A | GLY206 |
A | GLY207 |
A | SER208 |
A | SER258 |
A | LYS259 |
A | THR260 |
A | THR263 |
A | GLN407 |
site_id | AC2 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE CIT B 5002 |
Chain | Residue |
B | ILE205 |
B | GLY207 |
B | SER208 |
B | SER258 |
B | LYS259 |
B | THR260 |
B | THR263 |
B | GLN407 |
B | HOH7009 |
B | HOH7237 |
B | HOH7258 |
B | HOH7277 |
B | HOH7361 |
B | HOH7400 |
C | HIS442 |
site_id | AC3 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE CIT C 5003 |
Chain | Residue |
B | HIS442 |
C | ILE205 |
C | GLY207 |
C | SER208 |
C | SER258 |
C | LYS259 |
C | THR260 |
C | THR263 |
C | GLN407 |
C | HOH7046 |
C | HOH7140 |
C | HOH7315 |
site_id | AC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL A 7001 |
Chain | Residue |
A | THR77 |
A | ASP78 |
A | ARG81 |
A | TYR85 |
A | ASP110 |
A | HOH7123 |
A | HOH7339 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL B 7002 |
Chain | Residue |
B | HIS74 |
B | ASP78 |
B | ARG81 |
B | TYR85 |
B | ASP110 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL C 7003 |
Chain | Residue |
C | THR77 |
C | ASP78 |
C | ARG81 |
C | TYR85 |
C | ASP110 |
C | HOH7215 |
Functional Information from PROSITE/UniProt
site_id | PS00174 |
Number of Residues | 18 |
Details | P_GLUCOSE_ISOMERASE_2 Phosphoglucose isomerase signature 2. GaIWgidsYDQwGVElgK |
Chain | Residue | Details |
A | GLY554-LYS571 |
site_id | PS00765 |
Number of Residues | 14 |
Details | P_GLUCOSE_ISOMERASE_1 Phosphoglucose isomerase signature 1. DwVGGRYSMwSAIG |
Chain | Residue | Details |
A | ASP321-GLY334 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 3 |
Details | ACT_SITE: Proton donor => ECO:0000250 |
Chain | Residue | Details |
A | GLU411 | |
B | GLU411 | |
C | GLU411 |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | ACT_SITE: ACT_SITE => ECO:0000250 |
Chain | Residue | Details |
A | HIS442 | |
A | LYS571 | |
B | HIS442 | |
B | LYS571 | |
C | HIS442 | |
C | LYS571 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 6 |
Details | Annotated By Reference To The Literature 1dqr |
Chain | Residue | Details |
A | GLY325 | |
A | LYS259 | |
A | ARG326 | |
A | GLU411 | |
A | GLU265 | |
A | LYS571 |
site_id | CSA2 |
Number of Residues | 6 |
Details | Annotated By Reference To The Literature 1dqr |
Chain | Residue | Details |
B | GLY325 | |
B | LYS259 | |
B | ARG326 | |
B | GLU411 | |
B | GLU265 | |
B | LYS571 |
site_id | CSA3 |
Number of Residues | 6 |
Details | Annotated By Reference To The Literature 1dqr |
Chain | Residue | Details |
C | GLY325 | |
C | LYS259 | |
C | ARG326 | |
C | GLU411 | |
C | GLU265 | |
C | LYS571 |
site_id | CSA4 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1dqr |
Chain | Residue | Details |
A | HIS442 |
site_id | CSA5 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1dqr |
Chain | Residue | Details |
B | HIS442 |
site_id | CSA6 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1dqr |
Chain | Residue | Details |
C | HIS442 |