Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004807 | molecular_function | triose-phosphate isomerase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006094 | biological_process | gluconeogenesis |
| A | 0006096 | biological_process | glycolytic process |
| A | 0016853 | molecular_function | isomerase activity |
| B | 0004807 | molecular_function | triose-phosphate isomerase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006094 | biological_process | gluconeogenesis |
| B | 0006096 | biological_process | glycolytic process |
| B | 0016853 | molecular_function | isomerase activity |
| C | 0004807 | molecular_function | triose-phosphate isomerase activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0006094 | biological_process | gluconeogenesis |
| C | 0006096 | biological_process | glycolytic process |
| C | 0016853 | molecular_function | isomerase activity |
| D | 0004807 | molecular_function | triose-phosphate isomerase activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0006094 | biological_process | gluconeogenesis |
| D | 0006096 | biological_process | glycolytic process |
| D | 0016853 | molecular_function | isomerase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | binding site for residue G3P A 301 |
| Chain | Residue |
| A | ASN7 |
| A | ALA196 |
| A | SER197 |
| A | HOH411 |
| A | HOH425 |
| A | HOH429 |
| A | LYS9 |
| A | HIS89 |
| A | GLU137 |
| A | ILE142 |
| A | GLY143 |
| A | ALA174 |
| A | GLY175 |
| A | LEU194 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | binding site for residue CL A 302 |
| Chain | Residue |
| A | ARG12 |
| A | LYS201 |
| site_id | AC3 |
| Number of Residues | 14 |
| Details | binding site for residue G3P B 301 |
| Chain | Residue |
| B | ASN7 |
| B | LYS9 |
| B | HIS89 |
| B | GLU137 |
| B | GLY143 |
| B | ALA174 |
| B | GLY175 |
| B | LEU194 |
| B | VAL195 |
| B | ALA196 |
| B | SER197 |
| B | HOH417 |
| B | HOH420 |
| B | HOH422 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue CL B 302 |
| Chain | Residue |
| B | ARG12 |
| B | LYS201 |
| B | HOH468 |
| site_id | AC5 |
| Number of Residues | 14 |
| Details | binding site for residue G3P C 301 |
| Chain | Residue |
| C | ASN7 |
| C | LYS9 |
| C | HIS89 |
| C | GLU137 |
| C | ILE142 |
| C | GLY143 |
| C | ALA174 |
| C | GLY175 |
| C | LEU194 |
| C | ALA196 |
| C | SER197 |
| C | HOH404 |
| C | HOH432 |
| C | HOH440 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue CL C 302 |
| Chain | Residue |
| C | TYR11 |
| C | ARG12 |
| C | LYS201 |
| C | HOH475 |
| site_id | AC7 |
| Number of Residues | 14 |
| Details | binding site for residue G3P D 301 |
| Chain | Residue |
| D | ASN7 |
| D | LYS9 |
| D | HIS89 |
| D | GLU137 |
| D | ILE142 |
| D | GLY143 |
| D | ALA174 |
| D | GLY175 |
| D | LEU194 |
| D | ALA196 |
| D | SER197 |
| D | HOH410 |
| D | HOH419 |
| D | HOH430 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | binding site for residue CL D 302 |
| Chain | Residue |
| D | ARG12 |
| D | LYS201 |
| D | HOH489 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Electrophile","evidences":[{"source":"HAMAP-Rule","id":"MF_00147","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00147","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 20 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00147","evidenceCode":"ECO:0000255"}]} |
