1Y7U
Crystal Structure of Acyl-Coa hydrolase from Bacillus cereus
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006637 | biological_process | acyl-CoA metabolic process |
| A | 0009062 | biological_process | fatty acid catabolic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016790 | molecular_function | thiolester hydrolase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0047617 | molecular_function | fatty acyl-CoA hydrolase activity |
| A | 0052816 | molecular_function | long-chain fatty acyl-CoA hydrolase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006637 | biological_process | acyl-CoA metabolic process |
| B | 0009062 | biological_process | fatty acid catabolic process |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016790 | molecular_function | thiolester hydrolase activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0047617 | molecular_function | fatty acyl-CoA hydrolase activity |
| B | 0052816 | molecular_function | long-chain fatty acyl-CoA hydrolase activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005829 | cellular_component | cytosol |
| C | 0006637 | biological_process | acyl-CoA metabolic process |
| C | 0009062 | biological_process | fatty acid catabolic process |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0016790 | molecular_function | thiolester hydrolase activity |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0047617 | molecular_function | fatty acyl-CoA hydrolase activity |
| C | 0052816 | molecular_function | long-chain fatty acyl-CoA hydrolase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA A 205 |
| Chain | Residue |
| A | THR11 |
| A | ALA12 |
| A | ASN13 |
| A | ASP137 |
| A | GLU141 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 B 206 |
| Chain | Residue |
| B | ARG74 |
| B | ARG110 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 207 |
| Chain | Residue |
| A | ARG110 |
| A | PRO72 |
| A | ARG74 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 C 208 |
| Chain | Residue |
| C | PRO72 |
| C | ARG74 |
| C | ARG110 |
| C | HOH211 |
| site_id | AC5 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE COA A 201 |
| Chain | Residue |
| A | VAL60 |
| A | THR61 |
| A | ALA62 |
| A | SER63 |
| A | GLY89 |
| A | ARG90 |
| A | THR91 |
| A | SER92 |
| A | THR118 |
| A | VAL120 |
| A | PRO128 |
| A | ARG155 |
| A | LYS159 |
| A | HOH228 |
| C | THR33 |
| C | LEU34 |
| C | ASP68 |
| C | PHE69 |
| C | LEU70 |
| C | HIS71 |
| C | PRO72 |
| C | VAL73 |
| C | HOH243 |
| C | HOH244 |
| site_id | AC6 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE COA B 202 |
| Chain | Residue |
| B | THR33 |
| B | LEU34 |
| B | ILE39 |
| B | VAL60 |
| B | THR61 |
| B | ALA62 |
| B | SER63 |
| B | ASP68 |
| B | PHE69 |
| B | HIS71 |
| B | VAL73 |
| B | GLY89 |
| B | ARG90 |
| B | THR91 |
| B | SER92 |
| B | THR118 |
| B | VAL120 |
| B | PRO128 |
| B | ARG155 |
| B | LYS159 |
| B | HOH216 |
| B | HOH224 |
| B | HOH233 |
| site_id | AC7 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE COA C 203 |
| Chain | Residue |
| A | THR33 |
| A | LEU34 |
| A | ILE39 |
| A | ASP68 |
| A | PHE69 |
| A | HIS71 |
| A | VAL73 |
| C | VAL60 |
| C | THR61 |
| C | SER63 |
| C | GLY89 |
| C | ARG90 |
| C | THR91 |
| C | SER92 |
| C | THR118 |
| C | VAL120 |
| C | PRO128 |
| C | ARG155 |
| C | LYS159 |
| C | HOH230 |
