1VAY
Crystal Structure of Uricase from Arthrobacter globiformis with inhibitor 8-azaxanthine
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004846 | molecular_function | urate oxidase activity |
| A | 0006144 | biological_process | purine nucleobase metabolic process |
| B | 0004846 | molecular_function | urate oxidase activity |
| B | 0006144 | biological_process | purine nucleobase metabolic process |
| C | 0004846 | molecular_function | urate oxidase activity |
| C | 0006144 | biological_process | purine nucleobase metabolic process |
| D | 0004846 | molecular_function | urate oxidase activity |
| D | 0006144 | biological_process | purine nucleobase metabolic process |
| E | 0004846 | molecular_function | urate oxidase activity |
| E | 0006144 | biological_process | purine nucleobase metabolic process |
| F | 0004846 | molecular_function | urate oxidase activity |
| F | 0006144 | biological_process | purine nucleobase metabolic process |
| G | 0004846 | molecular_function | urate oxidase activity |
| G | 0006144 | biological_process | purine nucleobase metabolic process |
| H | 0004846 | molecular_function | urate oxidase activity |
| H | 0006144 | biological_process | purine nucleobase metabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE AZA B 1301 |
| Chain | Residue |
| B | PHE163 |
| C | HOH349 |
| B | ARG180 |
| B | LEU222 |
| B | GLN223 |
| B | ASN249 |
| B | HOH1388 |
| C | TYR20 |
| C | VAL64 |
| C | THR67 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE AZA D 1302 |
| Chain | Residue |
| A | TYR20 |
| A | VAL64 |
| A | ALA66 |
| A | THR67 |
| D | PHE163 |
| D | LEU174 |
| D | ARG180 |
| D | LEU222 |
| D | GLN223 |
| D | ASN249 |
| D | HOH1335 |
| site_id | AC3 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE AZA B 1303 |
| Chain | Residue |
| B | TYR20 |
| B | VAL64 |
| B | ALA66 |
| B | THR67 |
| B | HOH1373 |
| C | PHE163 |
| C | ARG180 |
| C | ALA221 |
| C | LEU222 |
| C | GLN223 |
| C | ASN249 |
| site_id | AC4 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE AZA A 1304 |
| Chain | Residue |
| A | PHE163 |
| A | LEU174 |
| A | ARG180 |
| A | ALA221 |
| A | LEU222 |
| A | GLN223 |
| A | HOH1425 |
| D | TYR20 |
| D | VAL64 |
| D | ALA66 |
| D | THR67 |
| site_id | AC5 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE AZA H 1305 |
| Chain | Residue |
| E | TYR20 |
| E | VAL64 |
| E | THR67 |
| H | PHE163 |
| H | LEU174 |
| H | ARG180 |
| H | ALA221 |
| H | LEU222 |
| H | GLN223 |
| H | ASN249 |
| site_id | AC6 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE AZA G 1306 |
| Chain | Residue |
| F | VAL64 |
| F | ALA66 |
| F | THR67 |
| G | PHE163 |
| G | LEU174 |
| G | ARG180 |
| G | ALA221 |
| G | LEU222 |
| G | GLN223 |
| G | ASN249 |
| G | HOH1428 |
| site_id | AC7 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE AZA F 1307 |
| Chain | Residue |
| F | PHE163 |
| F | ARG180 |
| F | ALA221 |
| F | LEU222 |
| F | GLN223 |
| F | ASN249 |
| F | HOH1418 |
| G | TYR20 |
| G | VAL64 |
| G | ALA66 |
| G | THR67 |
| site_id | AC8 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE AZA E 1308 |
| Chain | Residue |
| E | PHE163 |
| E | LEU174 |
| E | ARG180 |
| E | ALA221 |
| E | LEU222 |
| E | GLN223 |
| E | ASN249 |
| E | HOH1374 |
| H | TYR20 |
| H | VAL64 |
| H | THR67 |
| H | HOH1339 |
Functional Information from PROSITE/UniProt
| site_id | PS00366 |
| Number of Residues | 28 |
| Details | URICASE Uricase signature. LtVLKSTgSeFhgFprdkYttLqettdR |
| Chain | Residue | Details |
| A | LEU153-ARG180 |
