2YZD
Crystal structure of uricase from Arthrobacter globiformis in complex with 8-azaxanthin (inhibitor)
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 |
| E | 0004846 | molecular_function | urate oxidase activity |
| E | 0005777 | cellular_component | peroxisome |
| E | 0006144 | biological_process | purine nucleobase metabolic process |
| E | 0006145 | biological_process | purine nucleobase catabolic process |
| E | 0016491 | molecular_function | oxidoreductase activity |
| E | 0019628 | biological_process | urate catabolic process |
| F | 0004846 | molecular_function | urate oxidase activity |
| F | 0005777 | cellular_component | peroxisome |
| F | 0006144 | biological_process | purine nucleobase metabolic process |
| F | 0006145 | biological_process | purine nucleobase catabolic process |
| F | 0016491 | molecular_function | oxidoreductase activity |
| F | 0019628 | biological_process | urate catabolic process |
| G | 0004846 | molecular_function | urate oxidase activity |
| G | 0005777 | cellular_component | peroxisome |
| G | 0006144 | biological_process | purine nucleobase metabolic process |
| G | 0006145 | biological_process | purine nucleobase catabolic process |
| G | 0016491 | molecular_function | oxidoreductase activity |
| G | 0019628 | biological_process | urate catabolic process |
| H | 0004846 | molecular_function | urate oxidase activity |
| H | 0005777 | cellular_component | peroxisome |
| H | 0006144 | biological_process | purine nucleobase metabolic process |
| H | 0006145 | biological_process | purine nucleobase catabolic process |
| H | 0016491 | molecular_function | oxidoreductase activity |
| H | 0019628 | biological_process | urate catabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE AZA A 1301 |
| Chain | Residue |
| A | PHE163 |
| D | ALA66 |
| D | THR67 |
| A | LEU174 |
| A | ARG180 |
| A | ALA221 |
| A | LEU222 |
| A | GLN223 |
| A | ASN249 |
| A | HOH1428 |
| D | TYR20 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE AZA D 1302 |
| Chain | Residue |
| A | TYR20 |
| A | ALA66 |
| A | THR67 |
| D | PHE163 |
| D | ARG180 |
| D | ALA221 |
| D | LEU222 |
| D | GLN223 |
| D | ASN249 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE AZA B 1303 |
| Chain | Residue |
| B | PHE163 |
| B | LEU174 |
| B | ARG180 |
| B | ALA221 |
| B | LEU222 |
| B | GLN223 |
| B | ASN249 |
| C | TYR20 |
| C | ALA66 |
| C | THR67 |
| site_id | AC4 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE AZA C 1304 |
| Chain | Residue |
| B | TYR20 |
| B | ALA66 |
| B | THR67 |
| C | PHE163 |
| C | LEU174 |
| C | ARG180 |
| C | ALA221 |
| C | LEU222 |
| C | GLN223 |
| C | ASN249 |
| C | HOH1378 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE AZA E 1305 |
| Chain | Residue |
| E | PHE163 |
| E | ARG180 |
| E | ALA221 |
| E | LEU222 |
| E | GLN223 |
| E | ASN249 |
| E | HOH1363 |
| H | TYR20 |
| H | THR67 |
| site_id | AC6 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE AZA H 1306 |
| Chain | Residue |
| E | TYR20 |
| E | THR67 |
| H | PHE163 |
| H | LEU174 |
| H | ARG180 |
| H | ALA221 |
| H | LEU222 |
| H | GLN223 |
| H | ASN249 |
| H | HOH1410 |
| site_id | AC7 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE AZA F 1307 |
| Chain | Residue |
| F | PHE163 |
| F | LEU174 |
| F | ARG180 |
| F | ALA221 |
| F | LEU222 |
| F | GLN223 |
| F | ASN249 |
| F | HOH1335 |
| G | TYR20 |
| G | ALA66 |
| G | THR67 |
| site_id | AC8 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE AZA G 1308 |
| Chain | Residue |
| F | TYR20 |
| F | ALA66 |
| F | THR67 |
| G | PHE163 |
| G | LEU174 |
| G | ARG180 |
| G | ALA221 |
| G | LEU222 |
| G | GLN223 |
| G | ASN249 |
| G | HOH1386 |
Functional Information from PROSITE/UniProt
| site_id | PS00366 |
| Number of Residues | 28 |
| Details | URICASE Uricase signature. LtVLKSTgSeFhgFprdkYttLqettdR |
| Chain | Residue | Details |
| A | LEU153-ARG180 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 24 |
| Details | ACT_SITE: Charge relay system => ECO:0000305|PubMed:18645230 |
| Chain | Residue | Details |
| A | LYS22 | |
| A | THR67 | |
| A | HIS251 | |
| B | LYS22 | |
| B | THR67 | |
| B | HIS251 | |
| C | LYS22 | |
| C | THR67 | |
| C | HIS251 | |
| D | LYS22 | |
| D | THR67 | |
| D | HIS251 | |
| E | LYS22 | |
| E | THR67 | |
| E | HIS251 | |
| F | LYS22 | |
| F | THR67 | |
| F | HIS251 | |
| G | LYS22 | |
| G | THR67 | |
| G | HIS251 | |
| H | LYS22 | |
| H | THR67 | |
| H | HIS251 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 40 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:18645230, ECO:0007744|PDB:2YZB, ECO:0007744|PDB:2YZC |
| Chain | Residue | Details |
| B | ARG180 | |
| B | GLN223 | |
| C | THR67 | |
| C | ASP68 | |
| C | PHE163 | |
| C | ARG180 | |
| C | GLN223 | |
| D | THR67 | |
| D | ASP68 | |
| D | PHE163 | |
| D | ARG180 | |
| D | GLN223 | |
| E | THR67 | |
| E | ASP68 | |
| E | PHE163 | |
| E | ARG180 | |
| E | GLN223 | |
| F | THR67 | |
| F | ASP68 | |
| F | PHE163 | |
| F | ARG180 | |
| F | GLN223 | |
| G | THR67 | |
| G | ASP68 | |
| G | PHE163 | |
| G | ARG180 | |
| G | GLN223 | |
| H | THR67 | |
| H | ASP68 | |
| H | PHE163 | |
| H | ARG180 | |
| H | GLN223 | |
| A | ASP68 | |
| A | PHE163 | |
| A | ARG180 | |
| A | GLN223 | |
| B | THR67 | |
| B | ASP68 | |
| B | PHE163 | |
| A | THR67 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q00511 |
| Chain | Residue | Details |
| A | ASN249 | |
| B | ASN249 | |
| C | ASN249 | |
| D | ASN249 | |
| E | ASN249 | |
| F | ASN249 | |
| G | ASN249 | |
| H | ASN249 |
