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 | |
D | LYS22 | |
D | THR67 | |
D | HIS251 | |
E | LYS22 | |
E | THR67 | |
E | HIS251 | |
F | LYS22 | |
F | THR67 | |
F | HIS251 | |
G | LYS22 | |
A | THR67 | |
G | THR67 | |
G | HIS251 | |
H | LYS22 | |
H | THR67 | |
H | HIS251 | |
A | HIS251 | |
B | LYS22 | |
B | THR67 | |
B | HIS251 | |
C | LYS22 | |
C | THR67 | |
C | 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 |
A | THR67 | |
B | GLN223 | |
C | THR67 | |
C | ASP68 | |
C | PHE163 | |
C | ARG180 | |
C | GLN223 | |
D | THR67 | |
D | ASP68 | |
D | PHE163 | |
D | ARG180 | |
A | ASP68 | |
D | GLN223 | |
E | THR67 | |
E | ASP68 | |
E | PHE163 | |
E | ARG180 | |
E | GLN223 | |
F | THR67 | |
F | ASP68 | |
F | PHE163 | |
F | ARG180 | |
A | PHE163 | |
F | GLN223 | |
G | THR67 | |
G | ASP68 | |
G | PHE163 | |
G | ARG180 | |
G | GLN223 | |
H | THR67 | |
H | ASP68 | |
H | PHE163 | |
H | ARG180 | |
A | ARG180 | |
H | GLN223 | |
A | GLN223 | |
B | THR67 | |
B | ASP68 | |
B | PHE163 | |
B | ARG180 |
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 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1r51 |
Chain | Residue | Details |
A | ARG180 | |
A | GLN223 |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1r51 |
Chain | Residue | Details |
B | ARG180 | |
B | GLN223 |
site_id | CSA3 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1r51 |
Chain | Residue | Details |
C | ARG180 | |
C | GLN223 |
site_id | CSA4 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1r51 |
Chain | Residue | Details |
D | ARG180 | |
D | GLN223 |
site_id | CSA5 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1r51 |
Chain | Residue | Details |
E | ARG180 | |
E | GLN223 |
site_id | CSA6 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1r51 |
Chain | Residue | Details |
F | ARG180 | |
F | GLN223 |
site_id | CSA7 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1r51 |
Chain | Residue | Details |
G | ARG180 | |
G | GLN223 |
site_id | CSA8 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1r51 |
Chain | Residue | Details |
H | ARG180 | |
H | GLN223 |