Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004846 | molecular_function | urate oxidase activity |
A | 0005777 | cellular_component | peroxisome |
A | 0006144 | biological_process | purine nucleobase metabolic process |
A | 0006145 | biological_process | purine nucleobase catabolic process |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0019628 | biological_process | urate catabolic process |
B | 0004846 | molecular_function | urate oxidase activity |
B | 0005777 | cellular_component | peroxisome |
B | 0006144 | biological_process | purine nucleobase metabolic process |
B | 0006145 | biological_process | purine nucleobase catabolic process |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0019628 | biological_process | urate catabolic process |
C | 0004846 | molecular_function | urate oxidase activity |
C | 0005777 | cellular_component | peroxisome |
C | 0006144 | biological_process | purine nucleobase metabolic process |
C | 0006145 | biological_process | purine nucleobase catabolic process |
C | 0016491 | molecular_function | oxidoreductase activity |
C | 0019628 | biological_process | urate catabolic process |
D | 0004846 | molecular_function | urate oxidase activity |
D | 0005777 | cellular_component | peroxisome |
D | 0006144 | biological_process | purine nucleobase metabolic process |
D | 0006145 | biological_process | purine nucleobase catabolic process |
D | 0016491 | molecular_function | oxidoreductase activity |
D | 0019628 | biological_process | urate catabolic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE ACT B 401 |
Chain | Residue |
A | SER46 |
A | GLN109 |
B | LYS291 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ACT D 401 |
Chain | Residue |
C | THR68 |
D | PHE170 |
D | ARG187 |
D | HOH555 |
site_id | AC3 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE ACT D 402 |
Functional Information from PROSITE/UniProt
site_id | PS00366 |
Number of Residues | 28 |
Details | URICASE Uricase signature. LkVLKTTqSgFegFikdqFttLpevkdR |
Chain | Residue | Details |
A | LEU160-ARG187 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | LYS23 | |
D | LYS23 | |
D | THR68 | |
D | HIS264 | |
A | THR68 | |
A | HIS264 | |
B | LYS23 | |
B | THR68 | |
B | HIS264 | |
C | LYS23 | |
C | THR68 | |
C | HIS264 | |
Chain | Residue | Details |
A | THR68 | |
B | PHE170 | |
B | ARG187 | |
B | VAL235 | |
B | GLN236 | |
B | ASN262 | |
C | THR68 | |
C | ASP69 | |
C | PHE170 | |
C | ARG187 | |
C | VAL235 | |
A | ASP69 | |
C | GLN236 | |
C | ASN262 | |
D | THR68 | |
D | ASP69 | |
D | PHE170 | |
D | ARG187 | |
D | VAL235 | |
D | GLN236 | |
D | ASN262 | |
A | PHE170 | |
A | ARG187 | |
A | VAL235 | |
A | GLN236 | |
A | ASN262 | |
B | THR68 | |
B | ASP69 | |
Chain | Residue | Details |
A | ALA2 | |
B | ALA2 | |
C | ALA2 | |
D | ALA2 | |
Chain | Residue | Details |
A | LYS10 | |
C | LYS23 | |
C | LYS221 | |
C | LYS228 | |
D | LYS10 | |
D | LYS23 | |
D | LYS221 | |
D | LYS228 | |
A | LYS23 | |
A | LYS221 | |
A | LYS228 | |
B | LYS10 | |
B | LYS23 | |
B | LYS221 | |
B | LYS228 | |
C | LYS10 | |
Chain | Residue | Details |
A | LYS27 | |
B | LYS36 | |
B | LYS118 | |
B | LYS122 | |
B | LYS164 | |
B | LYS175 | |
B | LYS185 | |
B | LYS278 | |
C | LYS27 | |
C | LYS36 | |
C | LYS118 | |
A | LYS36 | |
C | LYS122 | |
C | LYS164 | |
C | LYS175 | |
C | LYS185 | |
C | LYS278 | |
D | LYS27 | |
D | LYS36 | |
D | LYS118 | |
D | LYS122 | |
D | LYS164 | |
A | LYS118 | |
D | LYS175 | |
D | LYS185 | |
D | LYS278 | |
A | LYS122 | |
A | LYS164 | |
A | LYS175 | |
A | LYS185 | |
A | LYS278 | |
B | LYS27 | |
Chain | Residue | Details |
A | SER39 | |
D | SER39 | |
D | SER63 | |
D | SER232 | |
A | SER63 | |
A | SER232 | |
B | SER39 | |
B | SER63 | |
B | SER232 | |
C | SER39 | |
C | SER63 | |
C | SER232 | |
Chain | Residue | Details |
A | TYR289 | |
B | TYR289 | |
C | TYR289 | |
D | TYR289 | |