5M2T
X-ray structure of uridine phosphorylase from Vibrio cholerae in complex with uridine at 1.03 A resolution
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004850 | molecular_function | uridine phosphorylase activity |
| A | 0005737 | cellular_component | cytoplasm |
| 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 | 0044206 | biological_process | UMP salvage |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004850 | molecular_function | uridine phosphorylase activity |
| B | 0005737 | cellular_component | cytoplasm |
| 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 | 0044206 | biological_process | UMP salvage |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0004850 | molecular_function | uridine phosphorylase activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0009116 | biological_process | nucleoside metabolic process |
| C | 0009164 | biological_process | nucleoside catabolic process |
| C | 0009166 | biological_process | nucleotide catabolic process |
| C | 0016757 | molecular_function | glycosyltransferase activity |
| C | 0016763 | molecular_function | pentosyltransferase activity |
| C | 0044206 | biological_process | UMP salvage |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0004850 | molecular_function | uridine phosphorylase activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0009116 | biological_process | nucleoside metabolic process |
| D | 0009164 | biological_process | nucleoside catabolic process |
| D | 0009166 | biological_process | nucleotide catabolic process |
| D | 0016757 | molecular_function | glycosyltransferase activity |
| D | 0016763 | molecular_function | pentosyltransferase activity |
| D | 0044206 | biological_process | UMP salvage |
| D | 0046872 | molecular_function | metal ion binding |
| E | 0003824 | molecular_function | catalytic activity |
| E | 0004850 | molecular_function | uridine phosphorylase activity |
| E | 0005737 | cellular_component | cytoplasm |
| E | 0009116 | biological_process | nucleoside metabolic process |
| E | 0009164 | biological_process | nucleoside catabolic process |
| E | 0009166 | biological_process | nucleotide catabolic process |
| E | 0016757 | molecular_function | glycosyltransferase activity |
| E | 0016763 | molecular_function | pentosyltransferase activity |
| E | 0044206 | biological_process | UMP salvage |
| E | 0046872 | molecular_function | metal ion binding |
| F | 0003824 | molecular_function | catalytic activity |
| F | 0004850 | molecular_function | uridine phosphorylase activity |
| F | 0005737 | cellular_component | cytoplasm |
| F | 0009116 | biological_process | nucleoside metabolic process |
| F | 0009164 | biological_process | nucleoside catabolic process |
| F | 0009166 | biological_process | nucleotide catabolic process |
| F | 0016757 | molecular_function | glycosyltransferase activity |
| F | 0016763 | molecular_function | pentosyltransferase activity |
| F | 0044206 | biological_process | UMP salvage |
| F | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 15 |
| Details | binding site for residue URI A 301 |
| Chain | Residue |
| A | THR93 |
| A | ILE220 |
| A | HOH422 |
| A | HOH429 |
| A | HOH491 |
| A | HOH514 |
| B | HIS7 |
| A | THR94 |
| A | GLY95 |
| A | PHE161 |
| A | GLN165 |
| A | ARG167 |
| A | GLU195 |
| A | MET196 |
| A | GLU197 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue NA A 302 |
| Chain | Residue |
| A | GLU48 |
| A | ILE68 |
| A | SER72 |
| B | GLU48 |
| B | ILE68 |
| B | SER72 |
| site_id | AC3 |
| Number of Residues | 18 |
| Details | binding site for residue URI B 301 |
| Chain | Residue |
| A | HIS7 |
| A | ARG47 |
| B | ILE68 |
| B | ARG90 |
| B | THR93 |
| B | THR94 |
| B | GLY95 |
| B | PHE161 |
| B | GLN165 |
| B | ARG167 |
| B | GLU195 |
| B | MET196 |
| B | GLU197 |
| B | ILE220 |
| B | HOH422 |
| B | HOH513 |
| B | HOH521 |
| B | HOH606 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue CL B 302 |
| Chain | Residue |
| A | HOH601 |
| B | GLY25 |
| B | ASP26 |
| B | ARG29 |
| site_id | AC5 |
| Number of Residues | 14 |
| Details | binding site for residue URI C 301 |
| Chain | Residue |
| C | THR93 |
| C | THR94 |
| C | GLY95 |
| C | PHE161 |
| C | GLN165 |
| C | ARG167 |
| C | GLU195 |
| C | MET196 |
| C | GLU197 |
| C | HOH434 |
| C | HOH463 |
| C | HOH530 |
| C | HOH573 |
| D | HIS7 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue CL C 302 |
| Chain | Residue |
| C | GLY25 |
| C | ASP26 |
| C | HOH471 |
| C | HOH581 |
| C | HOH617 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | binding site for residue CL C 303 |
| Chain | Residue |
| B | HOH540 |
| C | PHE133 |
| C | HOH532 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | binding site for residue NA C 304 |
| Chain | Residue |
| C | GLU48 |
| C | ILE68 |
| C | SER72 |
| D | GLU48 |
| D | ILE68 |
| D | SER72 |
| site_id | AC9 |
| Number of Residues | 14 |
| Details | binding site for residue URI D 301 |
| Chain | Residue |
| C | HIS7 |
| D | THR93 |
| D | THR94 |
| D | GLY95 |
| D | PHE161 |
| D | GLN165 |
| D | ARG167 |
| D | GLU195 |
| D | MET196 |
| D | GLU197 |
| D | HOH529 |
| D | HOH559 |
| D | HOH571 |
| D | HOH610 |
| site_id | AD1 |
| Number of Residues | 2 |
| Details | binding site for residue CL D 302 |
| Chain | Residue |
| D | PHE133 |
| E | HOH544 |
| site_id | AD2 |
| Number of Residues | 5 |
| Details | binding site for residue CL D 303 |
| Chain | Residue |
| C | HOH591 |
| D | GLY25 |
| D | ASP26 |
| D | ARG29 |
| D | HOH509 |
| site_id | AD3 |
| Number of Residues | 4 |
| Details | binding site for residue MG D 304 |
| Chain | Residue |
| D | HOH453 |
| D | HOH543 |
| D | HOH606 |
| D | HOH656 |
| site_id | AD4 |
| Number of Residues | 15 |
| Details | binding site for residue URI E 301 |
| Chain | Residue |
| E | PHE161 |
| E | GLN165 |
| E | ARG167 |
| E | GLU195 |
| E | MET196 |
| E | GLU197 |
| E | ILE220 |
| E | EDO303 |
| E | HOH532 |
| E | HOH569 |
| F | HIS7 |
| F | HOH418 |
| E | THR93 |
| E | THR94 |
| E | GLY95 |
| site_id | AD5 |
| Number of Residues | 6 |
| Details | binding site for residue NA E 302 |
| Chain | Residue |
| E | GLU48 |
| E | ILE68 |
| E | SER72 |
| F | GLU48 |
| F | ILE68 |
| F | SER72 |
| site_id | AD6 |
| Number of Residues | 8 |
| Details | binding site for residue EDO E 303 |
| Chain | Residue |
| E | ARG90 |
| E | GLY92 |
| E | THR93 |
| E | GLU197 |
| E | URI301 |
| E | HOH410 |
| E | HOH423 |
| F | ARG47 |
| site_id | AD7 |
| Number of Residues | 14 |
| Details | binding site for residue URI F 301 |
| Chain | Residue |
| E | HIS7 |
| F | THR93 |
| F | THR94 |
| F | GLY95 |
| F | PHE161 |
| F | GLN165 |
| F | ARG167 |
| F | GLU195 |
| F | MET196 |
| F | GLU197 |
| F | HOH443 |
| F | HOH490 |
| F | HOH554 |
| F | HOH604 |
| site_id | AD8 |
| Number of Residues | 4 |
| Details | binding site for residue CL F 302 |
| Chain | Residue |
| F | GLY25 |
| F | ASP26 |
| F | ARG29 |
| F | HOH644 |
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 | SER65-LEU80 |
