1XXJ
Urate oxidase from aspergillus flavus complexed with 5-amino 6-nitro uracil
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 | 10 |
Details | BINDING SITE FOR RESIDUE UNC A 999 |
Chain | Residue |
A | PHE159 |
B | HOH1001 |
A | ARG176 |
A | VAL227 |
A | GLN228 |
A | ASN254 |
B | ILE54 |
B | ALA56 |
B | THR57 |
B | ASP58 |
site_id | AC2 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE UNC B 1999 |
Chain | Residue |
A | ALA56 |
A | THR57 |
A | HOH1008 |
B | PHE159 |
B | ARG176 |
B | SER226 |
B | VAL227 |
B | GLN228 |
B | ASN254 |
site_id | AC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE UNC C 2999 |
Chain | Residue |
C | PHE159 |
C | ARG176 |
C | VAL227 |
C | GLN228 |
C | ASN254 |
D | ALA56 |
D | THR57 |
D | ASP58 |
site_id | AC4 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE UNC D 3999 |
Chain | Residue |
C | ILE54 |
C | ALA56 |
C | THR57 |
C | ASP58 |
D | PHE159 |
D | LEU170 |
D | ARG176 |
D | SER226 |
D | VAL227 |
D | GLN228 |
site_id | AC5 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE BNZ C 931 |
Chain | Residue |
C | TRP174 |
C | TRP174 |
Functional Information from PROSITE/UniProt
site_id | PS00366 |
Number of Residues | 28 |
Details | URICASE Uricase signature. LtVLKSTnSqFwgFlrdeYttLketwdR |
Chain | Residue | Details |
A | LEU149-ARG176 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 12 |
Details | ACT_SITE: Charge relay system => ECO:0000269|PubMed:24466188, ECO:0007744|PDB:4N3M, ECO:0007744|PDB:4N9M, ECO:0007744|PDB:4N9S, ECO:0007744|PDB:4N9V |
Chain | Residue | Details |
A | ASP11 | |
D | ASP11 | |
D | ASP58 | |
D | TYR257 | |
A | ASP58 | |
A | TYR257 | |
B | ASP11 | |
B | ASP58 | |
B | TYR257 | |
C | ASP11 | |
C | ASP58 | |
C | TYR257 |
Chain | Residue | Details |
A | ASP58 | |
B | ASP58 | |
C | ASP58 | |
D | ASP58 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000305|PubMed:9360612, ECO:0007744|PDB:1R4S, ECO:0007744|PDB:3LBG, ECO:0007744|PDB:3LD4, ECO:0007744|PDB:4CW0, ECO:0007744|PDB:4CW2, ECO:0007744|PDB:4CW3, ECO:0007744|PDB:4CW6, ECO:0007744|PDB:4N9S |
Chain | Residue | Details |
A | SER59 | |
B | SER59 | |
C | SER59 | |
D | SER59 |
Chain | Residue | Details |
A | TRP160 | |
B | TRP160 | |
C | TRP160 | |
D | TRP160 |
Chain | Residue | Details |
A | ILE177 | |
B | ILE177 | |
C | ILE177 | |
D | ILE177 |
Chain | Residue | Details |
A | GLN228 | |
B | GLN228 | |
C | GLN228 | |
D | GLN228 |
Chain | Residue | Details |
A | ALA229 | |
B | ALA229 | |
C | ALA229 | |
D | ALA229 |
site_id | SWS_FT_FI8 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0007744|PDB:4CW2, ECO:0007744|PDB:4CW3, ECO:0007744|PDB:4CW6 |
Chain | Residue | Details |
A | LYS255 | |
B | LYS255 | |
C | LYS255 | |
D | LYS255 |
site_id | SWS_FT_FI9 |
Number of Residues | 4 |
Details | MOD_RES: N-acetylserine => ECO:0000305|PubMed:1339455, ECO:0007744|PDB:1R4S, ECO:0007744|PDB:1R4U, ECO:0007744|PDB:1R51, ECO:0007744|PDB:1R56, ECO:0007744|PDB:1WRR, ECO:0007744|PDB:1WS2, ECO:0007744|PDB:1WS3, ECO:0007744|PDB:1XT4, ECO:0007744|PDB:1XXJ, ECO:0007744|PDB:1XY3, ECO:0007744|PDB:2FXL, ECO:0007744|PDB:3BJP, ECO:0007744|PDB:4FSK |
Chain | Residue | Details |
A | ALA2 | |
B | ALA2 | |
C | ALA2 | |
D | ALA2 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1r51 |
Chain | Residue | Details |
A | GLN228 | |
A | ARG176 |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1r51 |
Chain | Residue | Details |
B | GLN228 | |
B | ARG176 |
site_id | CSA3 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1r51 |
Chain | Residue | Details |
C | GLN228 | |
C | ARG176 |
site_id | CSA4 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1r51 |
Chain | Residue | Details |
D | GLN228 | |
D | ARG176 |
site_id | MCSA1 |
Number of Residues | 5 |
Details | M-CSA 118 |
Chain | Residue | Details |
A | ASP11 | hydrogen bond donor, proton acceptor, proton donor, proton relay |
A | ASP58 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
A | ILE177 | electrostatic stabiliser |
A | ALA229 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
A | TYR257 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
site_id | MCSA2 |
Number of Residues | 5 |
Details | M-CSA 118 |
Chain | Residue | Details |
B | ASP11 | hydrogen bond donor, proton acceptor, proton donor, proton relay |
B | ASP58 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
B | ILE177 | electrostatic stabiliser |
B | ALA229 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
B | TYR257 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
site_id | MCSA3 |
Number of Residues | 5 |
Details | M-CSA 118 |
Chain | Residue | Details |
C | ASP11 | hydrogen bond donor, proton acceptor, proton donor, proton relay |
C | ASP58 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
C | ILE177 | electrostatic stabiliser |
C | ALA229 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
C | TYR257 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
site_id | MCSA4 |
Number of Residues | 5 |
Details | M-CSA 118 |
Chain | Residue | Details |
D | ASP11 | hydrogen bond donor, proton acceptor, proton donor, proton relay |
D | ASP58 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
D | ILE177 | electrostatic stabiliser |
D | ALA229 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
D | TYR257 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |