4MAQ
Crystal Structure of a putative fumarylpyruvate hydrolase from Burkholderia cenocepacia
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0018773 | molecular_function | acetylpyruvate hydrolase activity |
| A | 0019628 | biological_process | urate catabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0050385 | molecular_function | ureidoglycolate lyase activity |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0018773 | molecular_function | acetylpyruvate hydrolase activity |
| B | 0019628 | biological_process | urate catabolic process |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0050385 | molecular_function | ureidoglycolate lyase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE EDO A 301 |
| Chain | Residue |
| A | THR55 |
| A | LYS56 |
| A | PRO57 |
| A | HOH425 |
| A | HOH703 |
| B | THR55 |
| B | LYS56 |
| B | PRO57 |
| B | HOH432 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO A 302 |
| Chain | Residue |
| A | GLU10 |
| A | ARG11 |
| A | SER13 |
| A | ARG22 |
| A | HOH423 |
| A | HOH491 |
| A | HOH606 |
