1RJQ
The crystal structure of the D-aminoacylase mutant D366A
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0016787 | molecular_function | hydrolase activity |
A | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
A | 0016811 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides |
A | 0046872 | molecular_function | metal ion binding |
A | 0047420 | molecular_function | N-acyl-D-amino-acid deacylase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE ACT A 901 |
Chain | Residue |
A | HIS67 |
A | ACT902 |
A | HIS69 |
A | CYS96 |
A | TYR192 |
A | HIS220 |
A | HIS250 |
A | SER289 |
A | THR290 |
A | ZN601 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ACT A 902 |
Chain | Residue |
A | LYS252 |
A | TYR283 |
A | GLY288 |
A | SER289 |
A | ARG377 |
A | ACT901 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 601 |
Chain | Residue |
A | CYS96 |
A | HIS220 |
A | HIS250 |
A | ACT901 |