6OFU
X-ray crystal structure of the YdjI aldolase from Escherichia coli K12
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005829 | cellular_component | cytosol |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0009025 | molecular_function | tagatose-bisphosphate aldolase activity |
| A | 0016832 | molecular_function | aldehyde-lyase activity |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0051289 | biological_process | protein homotetramerization |
| B | 0005829 | cellular_component | cytosol |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0009025 | molecular_function | tagatose-bisphosphate aldolase activity |
| B | 0016832 | molecular_function | aldehyde-lyase activity |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0051289 | biological_process | protein homotetramerization |
| C | 0005829 | cellular_component | cytosol |
| C | 0005975 | biological_process | carbohydrate metabolic process |
| C | 0008270 | molecular_function | zinc ion binding |
| C | 0009025 | molecular_function | tagatose-bisphosphate aldolase activity |
| C | 0016832 | molecular_function | aldehyde-lyase activity |
| C | 0042802 | molecular_function | identical protein binding |
| C | 0051289 | biological_process | protein homotetramerization |
| D | 0005829 | cellular_component | cytosol |
| D | 0005975 | biological_process | carbohydrate metabolic process |
| D | 0008270 | molecular_function | zinc ion binding |
| D | 0009025 | molecular_function | tagatose-bisphosphate aldolase activity |
| D | 0016832 | molecular_function | aldehyde-lyase activity |
| D | 0042802 | molecular_function | identical protein binding |
| D | 0051289 | biological_process | protein homotetramerization |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | binding site for residue ZN A 301 |
| Chain | Residue |
| A | HIS82 |
| A | HIS178 |
| A | HIS206 |
| A | HOH1134 |
| A | HOH1242 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | binding site for residue CL A 302 |
| Chain | Residue |
| A | ARG164 |
| A | HOH1269 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue ZN B 301 |
| Chain | Residue |
| B | HIS178 |
| B | HIS206 |
| B | HOH533 |
| B | HIS82 |
| B | GLU133 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | binding site for residue CL B 302 |
| Chain | Residue |
| B | ARG164 |
| B | HOH463 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue ZN C 301 |
| Chain | Residue |
| C | HIS82 |
| C | HIS206 |
| C | HOH451 |
| C | HOH559 |
| C | HOH578 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue ZN C 302 |
| Chain | Residue |
| C | HIS82 |
| C | ASP103 |
| C | GLU133 |
| C | HIS206 |
| C | HOH418 |
| C | HOH606 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue ZN D 301 |
| Chain | Residue |
| D | HIS82 |
| D | GLU133 |
| D | HIS206 |
| D | HOH416 |
| D | HOH587 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"UniProtKB","id":"P0AB71","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"PDB","id":"6OFU","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
