5H6G
Crystal structure of a thermostable lipase from Marine Streptomyces
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0016042 | biological_process | lipid catabolic process |
| A | 0016298 | molecular_function | lipase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0016042 | biological_process | lipid catabolic process |
| B | 0016298 | molecular_function | lipase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0016042 | biological_process | lipid catabolic process |
| C | 0016298 | molecular_function | lipase activity |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 2 |
| Details | binding site for residue PO4 A 301 |
| Chain | Residue |
| A | TYR206 |
| A | ARG207 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue K B 301 |
| Chain | Residue |
| B | ASP88 |
| B | ASP92 |
| C | ASP88 |
| C | ASP92 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue PO4 B 302 |
| Chain | Residue |
| B | LYS198 |
| B | TYR206 |
| B | ARG207 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue PO4 B 303 |
| Chain | Residue |
| B | TRP17 |
| B | ASN18 |
| B | ILE43 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | binding site for residue PO4 B 304 |
| Chain | Residue |
| B | PRO29 |
| B | ARG30 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | binding site for residue GOL C 301 |
| Chain | Residue |
| C | TRP17 |
| C | ASN18 |
| C | ILE43 |
