5KNU
Crystal structure of E. coli hypoxanthine phosphoribosyltransferase in complexed with 9-[N,N-(Bis-3-phosphonopropyl)aminomethyl]-9-deazahypoxanthine
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0000287 | molecular_function | magnesium ion binding |
| 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 | 0032991 | cellular_component | protein-containing complex |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0046100 | biological_process | hypoxanthine metabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051289 | biological_process | protein homotetramerization |
| A | 0052657 | molecular_function | guanine phosphoribosyltransferase activity |
| A | 0097216 | molecular_function | guanosine tetraphosphate binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| 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 | 0032991 | cellular_component | protein-containing complex |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0046100 | biological_process | hypoxanthine metabolic process |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051289 | biological_process | protein homotetramerization |
| B | 0052657 | molecular_function | guanine phosphoribosyltransferase activity |
| B | 0097216 | molecular_function | guanosine tetraphosphate binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | binding site for residue 6WA A 201 |
| Chain | Residue |
| A | ASP107 |
| A | ASP163 |
| A | HOH301 |
| A | HOH302 |
| A | HOH306 |
| A | HOH330 |
| A | SER108 |
| A | GLY109 |
| A | THR111 |
| A | LYS135 |
| A | GLU155 |
| A | PHE156 |
| A | VAL157 |
| A | ILE162 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 202 |
| Chain | Residue |
| A | GLU103 |
| A | ASP104 |
| A | HOH322 |
| A | HOH326 |
| A | HOH327 |
| A | HOH332 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue EPE A 203 |
| Chain | Residue |
| A | VAL11 |
| A | PRO14 |
| A | GLU15 |
| A | TYR173 |
| site_id | AC4 |
| Number of Residues | 16 |
| Details | binding site for residue 6WA B 201 |
| Chain | Residue |
| B | SER73 |
| B | ILE105 |
| B | ILE106 |
| B | ASP107 |
| B | SER108 |
| B | GLY109 |
| B | LEU112 |
| B | LYS135 |
| B | ARG138 |
| B | VAL157 |
| B | ILE162 |
| B | ASP163 |
| B | HOH301 |
| B | HOH305 |
| B | HOH311 |
| B | HOH321 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue MG B 202 |
| Chain | Residue |
| B | GLU103 |
| B | ASP104 |
| B | HOH325 |
| B | HOH327 |
| B | HOH331 |
Functional Information from PROSITE/UniProt
| site_id | PS00103 |
| Number of Residues | 13 |
| Details | PUR_PYR_PR_TRANSFER Purine/pyrimidine phosphoribosyl transferases signature. VLIVEDIIDSGnT |
| Chain | Residue | Details |
| A | VAL99-THR111 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor => ECO:0000305|PubMed:12070315 |
| Chain | Residue | Details |
| A | ASP107 | |
| B | ASP107 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P9WHQ9 |
| Chain | Residue | Details |
| A | ARG47 | |
| A | GLY48 | |
| A | ARG169 | |
| B | ARG47 | |
| B | GLY48 | |
| B | ARG169 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12070315, ECO:0007744|PDB:1GRV |
| Chain | Residue | Details |
| A | GLU103 | |
| A | ASP104 | |
| B | GLU103 | |
| B | ASP104 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12070315, ECO:0007744|PDB:1G9S |
| Chain | Residue | Details |
| A | ASP107 | |
| A | LYS135 | |
| B | ASP107 | |
| B | LYS135 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12070315, ECO:0007744|PDB:1G9T |
| Chain | Residue | Details |
| A | ASP163 | |
| B | ASP163 |
