3G02
Structure of enantioselective mutant of epoxide hydrolase from Aspergillus niger generated by directed evolution
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0004301 | molecular_function | epoxide hydrolase activity |
A | 0016787 | molecular_function | hydrolase activity |
A | 0016803 | molecular_function | ether hydrolase activity |
A | 0097176 | biological_process | epoxide metabolic process |
B | 0003824 | molecular_function | catalytic activity |
B | 0004301 | molecular_function | epoxide hydrolase activity |
B | 0016787 | molecular_function | hydrolase activity |
B | 0016803 | molecular_function | ether hydrolase activity |
B | 0097176 | biological_process | epoxide metabolic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE FMT A 408 |
Chain | Residue |
A | TRP117 |
A | ASP192 |
A | TYR251 |
A | TRP284 |
A | TYR314 |
A | TRP317 |
A | HOH495 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE FMT A 409 |
Chain | Residue |
A | CYS216 |
A | ASN217 |
A | TYR330 |
A | HOH496 |
A | SER195 |
A | ARG199 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE FMT B 408 |
Chain | Residue |
B | TRP117 |
B | ASP192 |
B | TYR251 |
B | TRP284 |
B | TYR314 |
B | TRP317 |