1EHY
X-ray structure of the epoxide hydrolase from agrobacterium radiobacter ad1
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0016787 | molecular_function | hydrolase activity |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0016787 | molecular_function | hydrolase activity |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0016787 | molecular_function | hydrolase activity |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0016787 | molecular_function | hydrolase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K A 295 |
| Chain | Residue |
| A | ASP181 |
| A | SER184 |
| A | TYR185 |
| A | ARG186 |
| A | HOH352 |
| A | HOH411 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE K B 296 |
| Chain | Residue |
| B | HOH359 |
| B | HOH440 |
| B | ASP181 |
| B | SER184 |
| B | ARG186 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE K C 297 |
| Chain | Residue |
| C | ASP181 |
| C | SER184 |
| C | TYR185 |
| C | ARG186 |
| C | HOH559 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE K D 298 |
| Chain | Residue |
| D | ASP181 |
| D | SER184 |
| D | TYR185 |
| D | ARG186 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 7 |
| Details | M-CSA 847 |
| Chain | Residue | Details |
| A | TRP38 | electrostatic stabiliser |
| A | ASP107 | covalently attached, electrofuge, electrophile, increase acidity, nucleophile |
| A | PHE108 | electrostatic stabiliser |
| A | TYR152 | electrostatic stabiliser, increase basicity |
| A | TYR215 | proton acceptor, proton donor |
| A | ASP246 | electrostatic stabiliser, increase basicity |
| A | HIS275 | proton acceptor, proton donor |
| site_id | MCSA2 |
| Number of Residues | 7 |
| Details | M-CSA 847 |
| Chain | Residue | Details |
| B | TRP38 | electrostatic stabiliser |
| B | ASP107 | covalently attached, electrofuge, electrophile, increase acidity, nucleophile |
| B | PHE108 | electrostatic stabiliser |
| B | TYR152 | electrostatic stabiliser, increase basicity |
| B | TYR215 | proton acceptor, proton donor |
| B | ASP246 | electrostatic stabiliser, increase basicity |
| B | HIS275 | proton acceptor, proton donor |
| site_id | MCSA3 |
| Number of Residues | 7 |
| Details | M-CSA 847 |
| Chain | Residue | Details |
| C | TRP38 | electrostatic stabiliser |
| C | ASP107 | covalently attached, electrofuge, electrophile, increase acidity, nucleophile |
| C | PHE108 | electrostatic stabiliser |
| C | TYR152 | electrostatic stabiliser, increase basicity |
| C | TYR215 | proton acceptor, proton donor |
| C | ASP246 | electrostatic stabiliser, increase basicity |
| C | HIS275 | proton acceptor, proton donor |
| site_id | MCSA4 |
| Number of Residues | 7 |
| Details | M-CSA 847 |
| Chain | Residue | Details |
| D | TRP38 | electrostatic stabiliser |
| D | ASP107 | covalently attached, electrofuge, electrophile, increase acidity, nucleophile |
| D | PHE108 | electrostatic stabiliser |
| D | TYR152 | electrostatic stabiliser, increase basicity |
| D | TYR215 | proton acceptor, proton donor |
| D | ASP246 | electrostatic stabiliser, increase basicity |
| D | HIS275 | proton acceptor, proton donor |
