5XO8
Crystal structure of a novel ZEN lactonase mutant with ligand Z
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004806 | molecular_function | triglyceride lipase activity |
| A | 0046503 | biological_process | glycerolipid catabolic process |
| B | 0004806 | molecular_function | triglyceride lipase activity |
| B | 0046503 | biological_process | glycerolipid catabolic process |
| C | 0004806 | molecular_function | triglyceride lipase activity |
| C | 0046503 | biological_process | glycerolipid catabolic process |
| D | 0004806 | molecular_function | triglyceride lipase activity |
| D | 0046503 | biological_process | glycerolipid catabolic process |
| E | 0004806 | molecular_function | triglyceride lipase activity |
| E | 0046503 | biological_process | glycerolipid catabolic process |
| F | 0004806 | molecular_function | triglyceride lipase activity |
| F | 0046503 | biological_process | glycerolipid catabolic process |
| G | 0004806 | molecular_function | triglyceride lipase activity |
| G | 0046503 | biological_process | glycerolipid catabolic process |
| H | 0004806 | molecular_function | triglyceride lipase activity |
| H | 0046503 | biological_process | glycerolipid catabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 15 |
| Details | binding site for residue ZER A 301 |
| Chain | Residue |
| A | GLY35 |
| A | TYR189 |
| A | PRO190 |
| A | ILE193 |
| A | PRO194 |
| A | HIS243 |
| A | PHE244 |
| A | LEU36 |
| A | ALA105 |
| A | SER106 |
| A | ASN134 |
| A | LEU138 |
| A | SER157 |
| A | TYR160 |
| A | TRP185 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | binding site for residue ZER B 301 |
| Chain | Residue |
| B | ASP34 |
| B | GLY35 |
| B | ALA105 |
| B | SER106 |
| B | ASN134 |
| B | ILE137 |
| B | TYR160 |
| B | TRP185 |
| B | TYR189 |
| B | PRO190 |
| B | ILE193 |
| B | PRO194 |
| B | HIS243 |
| B | PHE244 |
| site_id | AC3 |
| Number of Residues | 12 |
| Details | binding site for residue ZER C 301 |
| Chain | Residue |
| C | GLY35 |
| C | ALA105 |
| C | SER106 |
| C | ASN134 |
| C | SER157 |
| C | TYR160 |
| C | TRP185 |
| C | TYR189 |
| C | PRO190 |
| C | PRO194 |
| C | HIS243 |
| C | PHE244 |
| site_id | AC4 |
| Number of Residues | 15 |
| Details | binding site for residue ZER D 301 |
| Chain | Residue |
| D | ASP34 |
| D | GLY35 |
| D | ALA105 |
| D | SER106 |
| D | ASN134 |
| D | MET153 |
| D | ASN156 |
| D | SER157 |
| D | TYR160 |
| D | TRP185 |
| D | TYR189 |
| D | PRO190 |
| D | PRO194 |
| D | HIS243 |
| D | PHE244 |
| site_id | AC5 |
| Number of Residues | 14 |
| Details | binding site for residue ZER E 301 |
| Chain | Residue |
| E | ASP34 |
| E | GLY35 |
| E | ALA105 |
| E | SER106 |
| E | ASN134 |
| E | MET153 |
| E | SER157 |
| E | TRP185 |
| E | TYR189 |
| E | PRO190 |
| E | ILE193 |
| E | PRO194 |
| E | HIS243 |
| E | PHE244 |
| site_id | AC6 |
| Number of Residues | 15 |
| Details | binding site for residue ZER F 301 |
| Chain | Residue |
| F | ASP34 |
| F | GLY35 |
| F | ALA105 |
| F | SER106 |
| F | ASN134 |
| F | MET153 |
| F | SER157 |
| F | TYR160 |
| F | TRP185 |
| F | TYR189 |
| F | PRO190 |
| F | ILE193 |
| F | PRO194 |
| F | HIS243 |
| F | PHE244 |
| site_id | AC7 |
| Number of Residues | 13 |
| Details | binding site for residue ZER G 301 |
| Chain | Residue |
| G | ASP34 |
| G | GLY35 |
| G | ALA105 |
| G | SER106 |
| G | ASN134 |
| G | LEU138 |
| G | SER157 |
| G | TRP185 |
| G | TYR189 |
| G | PRO190 |
| G | PRO194 |
| G | HIS243 |
| G | PHE244 |
| site_id | AC8 |
| Number of Residues | 14 |
| Details | binding site for residue ZER H 301 |
| Chain | Residue |
| H | GLY35 |
| H | ALA105 |
| H | SER106 |
| H | ASN134 |
| H | LEU138 |
| H | SER157 |
| H | TYR160 |
| H | TRP185 |
| H | TYR189 |
| H | PRO190 |
| H | PRO194 |
| H | HIS243 |
| H | PHE244 |
| H | ASP34 |
