Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0006212 | biological_process | uracil catabolic process |
A | 0016787 | molecular_function | hydrolase activity |
A | 0016812 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides |
A | 0046872 | molecular_function | metal ion binding |
A | 0047694 | molecular_function | barbiturase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 12 |
Details | binding site for residue WDL A 401 |
Chain | Residue |
A | GLY46 |
A | SER347 |
A | VAL348 |
A | HOH502 |
A | ARG53 |
A | SER83 |
A | GLY84 |
A | MET190 |
A | ASN194 |
A | SER230 |
A | SER231 |
A | LYS328 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue NA A 402 |
Chain | Residue |
A | GLU301 |
A | ALA350 |
A | GLN353 |
A | GLY354 |
A | PRO355 |
A | GLY358 |
site_id | AC3 |
Number of Residues | 2 |
Details | binding site for residue CL A 403 |
Chain | Residue |
A | ARG34 |
A | ALA102 |
Functional Information from PROSITE/UniProt
site_id | PS00136 |
Number of Residues | 12 |
Details | SUBTILASE_ASP Serine proteases, subtilase family, aspartic acid active site. AKLIDDGVleaD |
Chain | Residue | Details |
A | ALA22-ASP33 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | LYS162 | |
Chain | Residue | Details |
A | SER230 | |
Chain | Residue | Details |
A | ARG53 | |
A | GLY354 | |
A | PRO355 | |
A | GLY358 | |
A | SER83 | |
A | ASN194 | |
A | SER230 | |
A | GLU301 | |
A | LYS328 | |
A | SER347 | |
A | ALA350 | |
A | GLN353 | |
Chain | Residue | Details |
A | HIS324 | |