2Q8N
Crystal structure of Glucose-6-phosphate isomerase (EC 5.3.1.9) (TM1385) from Thermotoga maritima at 1.82 A resolution
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004347 | molecular_function | glucose-6-phosphate isomerase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006094 | biological_process | gluconeogenesis |
| A | 0006096 | biological_process | glycolytic process |
| 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 | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006094 | biological_process | gluconeogenesis |
| B | 0006096 | biological_process | glycolytic process |
| 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 |
| C | 0004347 | molecular_function | glucose-6-phosphate isomerase activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005829 | cellular_component | cytosol |
| C | 0006094 | biological_process | gluconeogenesis |
| C | 0006096 | biological_process | glycolytic process |
| C | 0016853 | molecular_function | isomerase activity |
| 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 | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 B 449 |
| Chain | Residue |
| B | ARG187 |
| B | HOH557 |
| C | ARG50 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 C 449 |
| Chain | Residue |
| C | SER138 |
| C | THR141 |
| C | LYS422 |
| C | HOH550 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 449 |
| Chain | Residue |
| A | LYS422 |
| A | HOH522 |
| A | HOH543 |
| A | SER138 |
| A | THR141 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 450 |
| Chain | Residue |
| B | SER138 |
| B | THR141 |
| B | LYS422 |
| B | HOH535 |
| B | HOH598 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 A 450 |
| Chain | Residue |
| A | THR97 |
| A | ARG98 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 C 450 |
| Chain | Residue |
| C | THR97 |
| C | ARG98 |
| C | HOH530 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL A 451 |
| Chain | Residue |
| A | LYS302 |
| A | HOH533 |
| B | LYS302 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL C 451 |
| Chain | Residue |
| C | LYS302 |
| C | HOH536 |
| site_id | AC9 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE 2PE C 452 |
| Chain | Residue |
| C | LEU82 |
| C | LEU82 |
| C | HIS85 |
| C | HIS85 |
| C | TYR86 |
| C | LEU91 |
| C | LEU91 |
| C | GLU95 |
| C | VAL107 |
| C | VAL107 |
| C | PHE108 |
| C | PHE108 |
| C | VAL109 |
| C | VAL109 |
| C | SER120 |
| C | SER120 |
| C | VAL121 |
| site_id | BC1 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE 2PE B 452 |
| Chain | Residue |
| A | LEU91 |
| A | GLU95 |
| A | VAL107 |
| A | PHE108 |
| A | VAL109 |
| A | SER120 |
| B | HIS85 |
| B | LEU91 |
| B | GLU95 |
| B | VAL107 |
| B | PHE108 |
| B | VAL109 |
| site_id | BC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE 2PE A 453 |
| Chain | Residue |
| A | ASN321 |
| B | PHE295 |
Functional Information from PROSITE/UniProt
| site_id | PS00174 |
| Number of Residues | 18 |
| Details | P_GLUCOSE_ISOMERASE_2 Phosphoglucose isomerase signature 2. GyLLeinpFDQpGVElgK |
| Chain | Residue | Details |
| A | GLY405-LYS422 |
| site_id | PS00230 |
| Number of Residues | 10 |
| Details | MAP1B_NEURAXIN Neuraxin and MAP1B proteins repeated region signature. GYtYEIKERS |
| Chain | Residue | Details |
| A | GLY433-SER442 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"HAMAP-Rule","id":"MF_00473","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"33422670","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Active site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00473","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"33422670","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1dqr |
| Chain | Residue | Details |
| C | LYS422 | |
| C | GLU281 | |
| C | ARG198 | |
| C | GLU143 | |
| C | GLY197 | |
| C | LYS137 |
| site_id | CSA2 |
| Number of Residues | 7 |
| Details | Annotated By Reference To The Literature 1dqr |
| Chain | Residue | Details |
| A | HIS310 | |
| B | GLU281 | |
| B | LYS422 | |
| B | GLU143 | |
| B | ARG198 | |
| B | GLY197 | |
| B | LYS137 |
| site_id | CSA3 |
| Number of Residues | 7 |
| Details | Annotated By Reference To The Literature 1dqr |
| Chain | Residue | Details |
| A | LYS422 | |
| A | GLU281 | |
| A | ARG198 | |
| A | GLU143 | |
| A | GLY197 | |
| A | LYS137 | |
| B | HIS310 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1dqr |
| Chain | Residue | Details |
| C | HIS310 |
