2O2C
Crystal structure of phosphoglucose isomerase from T. brucei containing glucose-6-phosphate in the active site
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004347 | molecular_function | glucose-6-phosphate isomerase activity |
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 | 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 | 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 | 20 |
Details | BINDING SITE FOR RESIDUE G6Q A 5001 |
Chain | Residue |
A | ILE205 |
A | ARG326 |
A | GLN407 |
A | GLU411 |
A | HIS442 |
A | GLN564 |
A | HOH7018 |
A | HOH7128 |
A | HOH7164 |
A | HOH7337 |
A | HOH7340 |
A | GLY206 |
A | HOH7363 |
A | GLY207 |
A | SER208 |
A | SER258 |
A | LYS259 |
A | THR260 |
A | THR263 |
A | GLY325 |
site_id | AC2 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE G6Q B 5002 |
Chain | Residue |
B | ILE205 |
B | GLY206 |
B | GLY207 |
B | SER208 |
B | SER258 |
B | LYS259 |
B | THR260 |
B | THR263 |
B | GLY325 |
B | ARG326 |
B | GLN407 |
B | GLU411 |
B | GLN564 |
B | HOH7012 |
B | HOH7112 |
B | HOH7288 |
B | HOH7318 |
B | HOH7325 |
B | HOH7362 |
B | HOH7373 |
B | HOH7447 |
C | HIS442 |
site_id | AC3 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE G6Q C 5003 |
Chain | Residue |
B | HIS442 |
C | ILE205 |
C | GLY207 |
C | SER208 |
C | SER258 |
C | LYS259 |
C | THR260 |
C | THR263 |
C | GLY325 |
C | ARG326 |
C | GLN407 |
C | GLU411 |
C | GLN564 |
C | HOH7014 |
C | HOH7105 |
C | HOH7243 |
C | HOH7257 |
C | HOH7261 |
C | HOH7273 |
site_id | AC4 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL A 7001 |
Chain | Residue |
A | THR77 |
A | ASP78 |
A | ARG81 |
A | TYR85 |
A | ASN109 |
A | ASP110 |
A | HOH7213 |
A | HOH7278 |
B | ASN588 |
site_id | AC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL A 7005 |
Chain | Residue |
A | LEU278 |
A | GLU288 |
A | LYS289 |
A | GLY290 |
A | SER291 |
A | VAL292 |
A | HOH7242 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL B 7002 |
Chain | Residue |
B | HIS74 |
B | THR77 |
B | ASP78 |
B | ARG81 |
B | ASP110 |
B | HOH7383 |
site_id | AC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL B 7004 |
Chain | Residue |
B | GLU188 |
B | TRP189 |
B | LYS190 |
B | LYS294 |
B | HOH7264 |
B | HOH7303 |
site_id | AC8 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL B 7006 |
Chain | Residue |
B | LYS220 |
B | GLN396 |
B | TYR397 |
B | TRP399 |
B | HOH7146 |
B | HOH7241 |
B | HOH7403 |
C | HIS239 |
C | GLU242 |
site_id | AC9 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL C 7003 |
Chain | Residue |
C | ASP78 |
C | ARG81 |
C | TYR85 |
C | ASN109 |
C | ASP110 |
C | HIS74 |
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 |