3OZG
Crystal Structure of Plasmodium falciparum Hypoxanthine-Guanine-Xanthine Phosphoribosyltransferase in complex with S-SerMe-ImmH phosphonate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0000310 | molecular_function | xanthine phosphoribosyltransferase activity |
| A | 0004422 | molecular_function | hypoxanthine phosphoribosyltransferase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006166 | biological_process | purine ribonucleoside salvage |
| A | 0006178 | biological_process | guanine salvage |
| A | 0016757 | molecular_function | glycosyltransferase activity |
| A | 0032263 | biological_process | GMP salvage |
| A | 0032264 | biological_process | IMP salvage |
| A | 0032265 | biological_process | XMP salvage |
| A | 0046100 | biological_process | hypoxanthine metabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0052657 | molecular_function | guanine phosphoribosyltransferase activity |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0000310 | molecular_function | xanthine phosphoribosyltransferase activity |
| B | 0004422 | molecular_function | hypoxanthine phosphoribosyltransferase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006166 | biological_process | purine ribonucleoside salvage |
| B | 0006178 | biological_process | guanine salvage |
| B | 0016757 | molecular_function | glycosyltransferase activity |
| B | 0032263 | biological_process | GMP salvage |
| B | 0032264 | biological_process | IMP salvage |
| B | 0032265 | biological_process | XMP salvage |
| B | 0046100 | biological_process | hypoxanthine metabolic process |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0052657 | molecular_function | guanine phosphoribosyltransferase activity |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0000287 | molecular_function | magnesium ion binding |
| C | 0000310 | molecular_function | xanthine phosphoribosyltransferase activity |
| C | 0004422 | molecular_function | hypoxanthine phosphoribosyltransferase activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005829 | cellular_component | cytosol |
| C | 0006166 | biological_process | purine ribonucleoside salvage |
| C | 0006178 | biological_process | guanine salvage |
| C | 0016757 | molecular_function | glycosyltransferase activity |
| C | 0032263 | biological_process | GMP salvage |
| C | 0032264 | biological_process | IMP salvage |
| C | 0032265 | biological_process | XMP salvage |
| C | 0046100 | biological_process | hypoxanthine metabolic process |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0052657 | molecular_function | guanine phosphoribosyltransferase activity |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0000287 | molecular_function | magnesium ion binding |
| D | 0000310 | molecular_function | xanthine phosphoribosyltransferase activity |
| D | 0004422 | molecular_function | hypoxanthine phosphoribosyltransferase activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005829 | cellular_component | cytosol |
| D | 0006166 | biological_process | purine ribonucleoside salvage |
| D | 0006178 | biological_process | guanine salvage |
| D | 0016757 | molecular_function | glycosyltransferase activity |
| D | 0032263 | biological_process | GMP salvage |
| D | 0032264 | biological_process | IMP salvage |
| D | 0032265 | biological_process | XMP salvage |
| D | 0046100 | biological_process | hypoxanthine metabolic process |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0052657 | molecular_function | guanine phosphoribosyltransferase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE SSI A 232 |
| Chain | Residue |
| A | TYR116 |
| A | LYS176 |
| A | PHE197 |
| A | VAL198 |
| A | ASP204 |
| A | POP233 |
| A | HOH237 |
| A | HOH250 |
| A | HOH269 |
| A | HOH291 |
| A | GLU144 |
| A | ASP145 |
| A | ILE146 |
| A | ASP148 |
| A | THR149 |
| A | GLY150 |
| A | LYS151 |
| A | THR152 |
| site_id | AC2 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE POP A 233 |
| Chain | Residue |
| A | LYS77 |
| A | GLY78 |
| A | ARG112 |
| A | VAL113 |
| A | LYS114 |
| A | SER115 |
| A | TYR116 |
| A | ASP204 |
| A | ARG210 |
| A | SSI232 |
| A | MG234 |
| A | HOH252 |
| A | HOH289 |
| A | HOH290 |
| A | HOH291 |
| A | HOH292 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 234 |
| Chain | Residue |
| A | ASP204 |
| A | POP233 |
| A | HOH269 |
| A | HOH289 |
| A | HOH290 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 232 |
| Chain | Residue |
| B | ASP204 |
| B | POP234 |
| B | HOH256 |
| B | HOH283 |
| B | HOH284 |
| site_id | AC5 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE SSI B 233 |
| Chain | Residue |
| B | TYR116 |
| B | GLU144 |
| B | ASP145 |
| B | ILE146 |
| B | ASP148 |
| B | THR149 |
| B | GLY150 |
| B | LYS151 |
| B | THR152 |
| B | LYS176 |
| B | PHE197 |
| B | VAL198 |
| B | ASP204 |
| B | POP234 |
| B | HOH256 |
| B | HOH266 |
| B | HOH280 |
| B | HOH285 |
| site_id | AC6 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE POP B 234 |
| Chain | Residue |
| B | LYS77 |
| B | GLY78 |
| B | ARG112 |
| B | VAL113 |
| B | LYS114 |
| B | SER115 |
| B | TYR116 |
| B | ASP204 |
| B | ARG210 |
| B | MG232 |
| B | SSI233 |
| B | HOH279 |
| B | HOH283 |
| B | HOH285 |
| B | HOH286 |
| site_id | AC7 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE SSI C 232 |
| Chain | Residue |
| C | TYR116 |
| C | GLU144 |
| C | ASP145 |
| C | ILE146 |
| C | ASP148 |
| C | THR149 |
| C | GLY150 |
| C | LYS151 |
| C | THR152 |
| C | LYS176 |
| C | PHE197 |
| C | VAL198 |
| C | LEU203 |
| C | ASP204 |
| C | POP233 |
| C | HOH265 |
| C | HOH270 |
| site_id | AC8 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE POP C 233 |
| Chain | Residue |
| C | LYS114 |
| C | SER115 |
| C | TYR116 |
| C | ASP204 |
| C | ARG210 |
| C | SSI232 |
| C | MG234 |
| C | HOH256 |
| C | HOH265 |
| C | HOH268 |
| C | HOH269 |
| C | HOH271 |
| C | HOH272 |
| C | LEU76 |
| C | LYS77 |
| C | GLY78 |
| C | ARG112 |
| C | VAL113 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG C 234 |
| Chain | Residue |
| C | ASP204 |
| C | POP233 |
| C | HOH268 |
| C | HOH269 |
| C | HOH270 |
| site_id | BC1 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE SSI D 232 |
| Chain | Residue |
| D | TYR116 |
| D | GLU144 |
| D | ASP145 |
| D | ILE146 |
| D | ASP148 |
| D | THR149 |
| D | GLY150 |
| D | LYS151 |
| D | THR152 |
| D | LYS176 |
| D | PHE197 |
| D | VAL198 |
| D | LEU203 |
| D | ASP204 |
| D | POP233 |
| D | HOH264 |
| D | HOH267 |
| D | HOH268 |
| D | HOH269 |
| D | HOH275 |
| site_id | BC2 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE POP D 233 |
| Chain | Residue |
| D | LYS77 |
| D | GLY78 |
| D | ARG112 |
| D | VAL113 |
| D | LYS114 |
| D | SER115 |
| D | TYR116 |
| D | ASP204 |
| D | ARG210 |
| D | SSI232 |
| D | MG234 |
| D | HOH244 |
| D | HOH265 |
| D | HOH266 |
| D | HOH268 |
| D | HOH269 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG D 234 |
| Chain | Residue |
| D | ASP204 |
| D | POP233 |
| D | HOH263 |
| D | HOH266 |
| D | HOH267 |
Functional Information from PROSITE/UniProt
| site_id | PS00103 |
| Number of Residues | 13 |
| Details | PUR_PYR_PR_TRANSFER Purine/pyrimidine phosphoribosyl transferases signature. VLIVEDIIDTGkT |
| Chain | Residue | Details |
| A | VAL140-THR152 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton acceptor => ECO:0000250 |
| Chain | Residue | Details |
| A | ASP148 | |
| B | ASP148 | |
| C | ASP148 | |
| D | ASP148 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | LYS77 | |
| D | LYS77 | |
| D | GLU144 | |
| D | LYS176 | |
| A | GLU144 | |
| A | LYS176 | |
| B | LYS77 | |
| B | GLU144 | |
| B | LYS176 | |
| C | LYS77 | |
| C | GLU144 | |
| C | LYS176 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10433693 |
| Chain | Residue | Details |
| A | ASP204 | |
| B | ASP204 | |
| C | ASP204 | |
| D | ASP204 |
