1TGV
Structure of E. coli Uridine Phosphorylase complexed with 5-Fluorouridine and sulfate
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0004850 | molecular_function | uridine phosphorylase activity |
A | 0005524 | molecular_function | ATP binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0006218 | biological_process | uridine catabolic process |
A | 0006974 | biological_process | DNA damage response |
A | 0009116 | biological_process | nucleoside metabolic process |
A | 0009164 | biological_process | nucleoside catabolic process |
A | 0009166 | biological_process | nucleotide catabolic process |
A | 0016757 | molecular_function | glycosyltransferase activity |
A | 0016763 | molecular_function | pentosyltransferase activity |
A | 0030955 | molecular_function | potassium ion binding |
A | 0032991 | cellular_component | protein-containing complex |
A | 0042802 | molecular_function | identical protein binding |
A | 0044206 | biological_process | UMP salvage |
A | 0046050 | biological_process | UMP catabolic process |
A | 0047847 | molecular_function | deoxyuridine phosphorylase activity |
B | 0003824 | molecular_function | catalytic activity |
B | 0004850 | molecular_function | uridine phosphorylase activity |
B | 0005524 | molecular_function | ATP binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0006218 | biological_process | uridine catabolic process |
B | 0006974 | biological_process | DNA damage response |
B | 0009116 | biological_process | nucleoside metabolic process |
B | 0009164 | biological_process | nucleoside catabolic process |
B | 0009166 | biological_process | nucleotide catabolic process |
B | 0016757 | molecular_function | glycosyltransferase activity |
B | 0016763 | molecular_function | pentosyltransferase activity |
B | 0030955 | molecular_function | potassium ion binding |
B | 0032991 | cellular_component | protein-containing complex |
B | 0042802 | molecular_function | identical protein binding |
B | 0044206 | biological_process | UMP salvage |
B | 0046050 | biological_process | UMP catabolic process |
B | 0047847 | molecular_function | deoxyuridine phosphorylase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SO4 A 482 |
Chain | Residue |
A | GLY26 |
A | ARG30 |
A | ARG91 |
A | ILE92 |
A | GLY93 |
A | THR94 |
A | 5UD3001 |
B | ARG48 |
site_id | AC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SO4 B 682 |
Chain | Residue |
B | GLY26 |
B | ARG30 |
B | ARG91 |
B | ILE92 |
B | GLY93 |
B | THR94 |
B | 5UD5002 |
A | ARG48 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE K A 1001 |
Chain | Residue |
A | GLU49 |
A | ILE69 |
A | SER73 |
B | GLU49 |
B | ILE69 |
B | SER73 |
site_id | AC4 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE 5UD A 3001 |
Chain | Residue |
A | ARG91 |
A | THR94 |
A | THR95 |
A | GLY96 |
A | PHE162 |
A | GLN166 |
A | ARG168 |
A | GLU196 |
A | MET197 |
A | GLU198 |
A | ILE220 |
A | VAL221 |
A | SO4482 |
A | HOH3032 |
A | HOH3035 |
B | PHE7 |
B | HIS8 |
site_id | AC5 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE 5UD B 5002 |
Chain | Residue |
A | HIS8 |
B | ILE69 |
B | ARG91 |
B | THR94 |
B | THR95 |
B | GLY96 |
B | PHE162 |
B | GLN166 |
B | ARG168 |
B | GLU196 |
B | MET197 |
B | GLU198 |
B | ILE220 |
B | VAL221 |
B | SO4682 |
B | HOH5020 |
B | HOH5084 |
Functional Information from PROSITE/UniProt
site_id | PS01232 |
Number of Residues | 16 |
Details | PNP_UDP_1 Purine and other phosphorylases family 1 signature. StGIGgPStSIaveEL |
Chain | Residue | Details |
A | SER66-LEU81 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1t0u |
Chain | Residue | Details |
A | GLU80 | |
A | HIS8 | |
A | ARG223 |
site_id | CSA2 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1t0u |
Chain | Residue | Details |
B | GLU80 | |
B | HIS8 | |
B | ARG223 |
site_id | MCSA1 |
Number of Residues | 4 |
Details | M-CSA 787 |
Chain | Residue | Details |
A | HIS8 | proton acceptor, proton donor |
A | GLU80 | electrostatic stabiliser, polar interaction |
A | ARG168 | proton acceptor, proton donor |
A | ARG223 | electrostatic stabiliser, polar interaction |
site_id | MCSA2 |
Number of Residues | 4 |
Details | M-CSA 787 |
Chain | Residue | Details |
B | HIS8 | proton acceptor, proton donor |
B | GLU80 | electrostatic stabiliser, polar interaction |
B | ARG168 | proton acceptor, proton donor |
B | ARG223 | electrostatic stabiliser, polar interaction |