1XY3
Urate oxidase from aspergillus flavus complexed with guanine
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 | 6 |
Details | BINDING SITE FOR RESIDUE GUN A 900 |
Chain | Residue |
A | PHE159 |
A | ARG176 |
A | VAL227 |
A | GLN228 |
B | ILE54 |
B | THR57 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GUN B 901 |
Chain | Residue |
B | ARG176 |
B | VAL227 |
B | GLN228 |
A | ALA56 |
A | THR57 |
B | PHE159 |
site_id | AC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GUN C 902 |
Chain | Residue |
C | PHE159 |
C | ARG176 |
C | VAL227 |
C | GLN228 |
D | ILE54 |
D | ALA56 |
D | THR57 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GUN D 903 |
Chain | Residue |
C | ILE54 |
C | THR57 |
D | PHE159 |
D | ARG176 |
D | VAL227 |
D | GLN228 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GUN E 904 |
Chain | Residue |
E | PHE159 |
E | ARG176 |
E | VAL227 |
E | GLN228 |
F | THR57 |
site_id | AC6 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GUN F 905 |
Chain | Residue |
E | ILE54 |
E | ALA56 |
E | THR57 |
F | PHE159 |
F | ARG176 |
F | VAL227 |
F | GLN228 |
site_id | AC7 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GUN G 906 |
Chain | Residue |
G | PHE159 |
G | ARG176 |
G | VAL227 |
G | GLN228 |
H | ILE54 |
H | ALA56 |
H | THR57 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GUN H 907 |
Chain | Residue |
G | THR57 |
H | PHE159 |
H | ARG176 |
H | VAL227 |
H | GLN228 |
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 | 24 |
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 | |
E | ASP11 | |
E | ASP58 | |
E | TYR257 | |
F | ASP11 | |
F | ASP58 | |
F | TYR257 | |
G | ASP11 | |
A | ASP58 | |
G | ASP58 | |
G | TYR257 | |
H | ASP11 | |
H | ASP58 | |
H | TYR257 | |
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 | |
E | ASP58 | |
F | ASP58 | |
G | ASP58 | |
H | ASP58 |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
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 | |
E | SER59 | |
F | SER59 | |
G | SER59 | |
H | SER59 |
Chain | Residue | Details |
A | TRP160 | |
B | TRP160 | |
C | TRP160 | |
D | TRP160 | |
E | TRP160 | |
F | TRP160 | |
G | TRP160 | |
H | TRP160 |
Chain | Residue | Details |
A | ILE177 | |
B | ILE177 | |
C | ILE177 | |
D | ILE177 | |
E | ILE177 | |
F | ILE177 | |
G | ILE177 | |
H | ILE177 |
Chain | Residue | Details |
A | GLN228 | |
B | GLN228 | |
C | GLN228 | |
D | GLN228 | |
E | GLN228 | |
F | GLN228 | |
G | GLN228 | |
H | GLN228 |
Chain | Residue | Details |
A | ALA229 | |
B | ALA229 | |
C | ALA229 | |
D | ALA229 | |
E | ALA229 | |
F | ALA229 | |
G | ALA229 | |
H | ALA229 |
site_id | SWS_FT_FI8 |
Number of Residues | 8 |
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 | |
E | LYS255 | |
F | LYS255 | |
G | LYS255 | |
H | LYS255 |
site_id | SWS_FT_FI9 |
Number of Residues | 8 |
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 | |
E | ALA2 | |
F | ALA2 | |
G | ALA2 | |
H | 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 | CSA5 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1r51 |
Chain | Residue | Details |
E | GLN228 | |
E | ARG176 |
site_id | CSA6 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1r51 |
Chain | Residue | Details |
F | GLN228 | |
F | ARG176 |
site_id | CSA7 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1r51 |
Chain | Residue | Details |
G | GLN228 | |
G | ARG176 |
site_id | CSA8 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1r51 |
Chain | Residue | Details |
H | GLN228 | |
H | 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 |
site_id | MCSA5 |
Number of Residues | 5 |
Details | M-CSA 118 |
Chain | Residue | Details |
E | ASP11 | hydrogen bond donor, proton acceptor, proton donor, proton relay |
E | ASP58 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
E | ILE177 | electrostatic stabiliser |
E | ALA229 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
E | TYR257 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
site_id | MCSA6 |
Number of Residues | 5 |
Details | M-CSA 118 |
Chain | Residue | Details |
F | ASP11 | hydrogen bond donor, proton acceptor, proton donor, proton relay |
F | ASP58 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
F | ILE177 | electrostatic stabiliser |
F | ALA229 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
F | TYR257 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
site_id | MCSA7 |
Number of Residues | 5 |
Details | M-CSA 118 |
Chain | Residue | Details |
G | ASP11 | hydrogen bond donor, proton acceptor, proton donor, proton relay |
G | ASP58 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
G | ILE177 | electrostatic stabiliser |
G | ALA229 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
G | TYR257 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
site_id | MCSA8 |
Number of Residues | 5 |
Details | M-CSA 118 |
Chain | Residue | Details |
H | ASP11 | hydrogen bond donor, proton acceptor, proton donor, proton relay |
H | ASP58 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
H | ILE177 | electrostatic stabiliser |
H | ALA229 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
H | TYR257 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |