6J3D
Crystal structure of acetolactate decarboxylase from Bacillus subtilis subspecies spizizenii in space group P21212
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016831 | molecular_function | carboxy-lyase activity |
| A | 0045151 | biological_process | acetoin biosynthetic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0047605 | molecular_function | acetolactate decarboxylase activity |
| B | 0016829 | molecular_function | lyase activity |
| B | 0016831 | molecular_function | carboxy-lyase activity |
| B | 0045151 | biological_process | acetoin biosynthetic process |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0047605 | molecular_function | acetolactate decarboxylase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue ZN A 301 |
| Chain | Residue |
| A | HIS191 |
| A | HIS193 |
| A | HIS204 |
| A | HOH406 |
| A | HOH430 |
| A | HOH542 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue ZN B 301 |
| Chain | Residue |
| B | HOH402 |
| B | HOH404 |
| B | HOH545 |
| B | HIS191 |
| B | HIS193 |
| B | HIS204 |
