Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004845 | molecular_function | uracil phosphoribosyltransferase activity |
A | 0005525 | molecular_function | GTP binding |
A | 0016757 | molecular_function | glycosyltransferase activity |
A | 0044206 | biological_process | UMP salvage |
B | 0004845 | molecular_function | uracil phosphoribosyltransferase activity |
B | 0005525 | molecular_function | GTP binding |
B | 0016757 | molecular_function | glycosyltransferase activity |
B | 0044206 | biological_process | UMP salvage |
C | 0004845 | molecular_function | uracil phosphoribosyltransferase activity |
C | 0005525 | molecular_function | GTP binding |
C | 0016757 | molecular_function | glycosyltransferase activity |
C | 0044206 | biological_process | UMP salvage |
D | 0004845 | molecular_function | uracil phosphoribosyltransferase activity |
D | 0005525 | molecular_function | GTP binding |
D | 0016757 | molecular_function | glycosyltransferase activity |
D | 0044206 | biological_process | UMP salvage |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PO4 D 899 |
Chain | Residue |
B | LYS59 |
D | LYS104 |
D | ARG129 |
D | ARG158 |
D | HOH1012 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PO4 C 899 |
Chain | Residue |
C | HOH1087 |
A | LYS59 |
C | LYS104 |
C | ARG129 |
C | ARG158 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE PO4 B 899 |
Chain | Residue |
B | LYS104 |
B | ARG129 |
B | ARG158 |
B | HOH1000 |
B | HOH1033 |
D | LYS59 |
site_id | AC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE PO4 A 899 |
Chain | Residue |
A | LYS104 |
A | ARG129 |
A | ARG158 |
A | HOH1002 |
A | HOH1036 |
A | HOH1041 |
C | LYS59 |
site_id | AC5 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE U5P D 999 |
Chain | Residue |
D | ARG137 |
D | ASP164 |
D | MET166 |
D | ALA168 |
D | THR169 |
D | ALA170 |
D | GLY171 |
D | SER172 |
D | TYR228 |
D | ILE229 |
D | GLY234 |
D | ASP235 |
D | PHE236 |
D | HOH1008 |
D | HOH1035 |
D | HOH1056 |
site_id | AC6 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE U5P C 999 |
Chain | Residue |
C | ARG137 |
C | ASP164 |
C | MET166 |
C | ALA168 |
C | THR169 |
C | ALA170 |
C | GLY171 |
C | SER172 |
C | TYR228 |
C | ILE229 |
C | GLY234 |
C | ASP235 |
C | PHE236 |
C | HOH1005 |
C | HOH1006 |
C | HOH1036 |
C | HOH1106 |
site_id | AC7 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE U5P B 999 |
Chain | Residue |
B | ALA113 |
B | ARG137 |
B | ASP164 |
B | MET166 |
B | ALA168 |
B | THR169 |
B | ALA170 |
B | GLY171 |
B | SER172 |
B | TYR228 |
B | ILE229 |
B | GLY234 |
B | ASP235 |
B | PHE236 |
B | HOH1002 |
B | HOH1007 |
B | HOH1082 |
C | HOH1119 |
site_id | AC8 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE U5P A 999 |
Chain | Residue |
A | ASP164 |
A | MET166 |
A | ALA168 |
A | THR169 |
A | ALA170 |
A | GLY171 |
A | SER172 |
A | TYR228 |
A | ILE229 |
A | GLY234 |
A | ASP235 |
A | PHE236 |
A | HOH1019 |
A | HOH1026 |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
D | LYS59 | |
C | LYS59 | |
B | LYS59 | |
A | LYS59 | |
Chain | Residue | Details |
D | ARG68 | |
D | TYR102 | |
C | ARG68 | |
C | TYR102 | |
B | ARG68 | |
B | TYR102 | |
A | ARG68 | |
A | TYR102 | |
Chain | Residue | Details |
D | ARG112 | |
C | ARG112 | |
B | ARG112 | |
A | ARG112 | |
Chain | Residue | Details |
D | ARG129 | |
A | ARG129 | |
A | ARG137 | |
A | ARG158 | |
D | ARG137 | |
D | ARG158 | |
C | ARG129 | |
C | ARG137 | |
C | ARG158 | |
B | ARG129 | |
B | ARG137 | |
B | ARG158 | |
Chain | Residue | Details |
D | ASP164 | |
C | ASP164 | |
B | ASP164 | |
A | ASP164 | |
Chain | Residue | Details |
D | ILE229 | |
D | GLY234 | |
C | ILE229 | |
C | GLY234 | |
B | ILE229 | |
B | GLY234 | |
A | ILE229 | |
A | GLY234 | |
Chain | Residue | Details |
D | ASP235 | |
C | ASP235 | |
B | ASP235 | |
A | ASP235 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1bd3 |
Chain | Residue | Details |
D | THR141 | |
D | ARG137 | |
D | ASP235 | |
site_id | CSA2 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1bd3 |
Chain | Residue | Details |
C | THR141 | |
C | ARG137 | |
C | ASP235 | |
site_id | CSA3 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1bd3 |
Chain | Residue | Details |
B | THR141 | |
B | ARG137 | |
B | ASP235 | |
site_id | CSA4 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1bd3 |
Chain | Residue | Details |
A | THR141 | |
A | ARG137 | |
A | ASP235 | |
site_id | MCSA1 |
Number of Residues | 4 |
Details | M-CSA 420 |
Chain | Residue | Details |
D | ARG137 | electrostatic stabiliser |
D | THR141 | electrostatic stabiliser |
D | ASP235 | electrostatic stabiliser |
D | ASP238 | modifies pKa |
site_id | MCSA2 |
Number of Residues | 4 |
Details | M-CSA 420 |
Chain | Residue | Details |
C | ARG137 | electrostatic stabiliser |
C | THR141 | electrostatic stabiliser |
C | ASP235 | electrostatic stabiliser |
C | ASP238 | modifies pKa |
site_id | MCSA3 |
Number of Residues | 4 |
Details | M-CSA 420 |
Chain | Residue | Details |
B | ARG137 | electrostatic stabiliser |
B | THR141 | electrostatic stabiliser |
B | ASP235 | electrostatic stabiliser |
B | ASP238 | modifies pKa |
site_id | MCSA4 |
Number of Residues | 4 |
Details | M-CSA 420 |
Chain | Residue | Details |
A | ARG137 | electrostatic stabiliser |
A | THR141 | electrostatic stabiliser |
A | ASP235 | electrostatic stabiliser |
A | ASP238 | modifies pKa |