6M53
Crystal structure of 2, 3-dihydroxybenzoic acid decarboxylase from Fusarium oxysporum
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016831 | molecular_function | carboxy-lyase activity |
| A | 0019748 | biological_process | secondary metabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016829 | molecular_function | lyase activity |
| B | 0016831 | molecular_function | carboxy-lyase activity |
| B | 0019748 | biological_process | secondary metabolic process |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005829 | cellular_component | cytosol |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0016829 | molecular_function | lyase activity |
| C | 0016831 | molecular_function | carboxy-lyase activity |
| C | 0019748 | biological_process | secondary metabolic process |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005829 | cellular_component | cytosol |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0016829 | molecular_function | lyase activity |
| D | 0016831 | molecular_function | carboxy-lyase activity |
| D | 0019748 | biological_process | secondary metabolic process |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue ZN A 401 |
| Chain | Residue |
| A | GLU9 |
| A | HIS168 |
| A | ASP292 |
| A | HOH736 |
| A | HOH741 |
| A | HOH795 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | binding site for residue GOL B 401 |
| Chain | Residue |
| B | HOH635 |
| B | HOH649 |
| B | HOH758 |
| D | LEU180 |
| D | GLN196 |
| B | ILE176 |
| B | TRP181 |
| B | GLN196 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue GOL B 402 |
| Chain | Residue |
| A | ARG20 |
| A | HOH570 |
| B | LEU3 |
| B | GLN334 |
| B | ASP337 |
| B | HIS339 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue ZN B 403 |
| Chain | Residue |
| B | GLU9 |
| B | HIS168 |
| B | ASP292 |
| B | HOH585 |
| B | HOH759 |
| B | HOH777 |
| site_id | AC5 |
| Number of Residues | 10 |
| Details | binding site for residue GOL C 401 |
| Chain | Residue |
| A | LEU180 |
| A | GLN196 |
| C | ILE176 |
| C | TRP181 |
| C | GLN196 |
| C | HOH596 |
| C | HOH640 |
| C | HOH649 |
| C | HOH654 |
| C | HOH704 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue ZN C 402 |
| Chain | Residue |
| C | GLU9 |
| C | HIS168 |
| C | ASP292 |
| C | HOH603 |
| C | HOH678 |
| C | HOH766 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue ZN D 401 |
| Chain | Residue |
| D | GLU9 |
| D | HIS168 |
| D | ASP292 |
| D | HOH584 |
| D | HOH717 |
