1YFZ
Novel IMP Binding in Feedback Inhibition of Hypoxanthine-Guanine Phosphoribosyltransferase from Thermoanaerobacter tengcongensis
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 | 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 | 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 | 0046100 | biological_process | hypoxanthine metabolic process |
B | 0046872 | molecular_function | metal ion binding |
B | 0052657 | molecular_function | guanine phosphoribosyltransferase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE ACT A 1200 |
Chain | Residue |
A | ILE103 |
A | ASP105 |
A | SER106 |
A | GLY107 |
A | LEU108 |
A | THR109 |
A | LEU110 |
A | HOH1281 |
site_id | AC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE ACT B 2200 |
Chain | Residue |
B | ASP105 |
B | SER106 |
B | GLY107 |
B | LEU108 |
B | THR109 |
B | LEU110 |
B | HOH2294 |
B | ILE103 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG B 2191 |
Chain | Residue |
B | GLU101 |
B | ASP102 |
B | HOH2273 |
B | HOH2279 |
B | HOH2285 |
B | HOH2288 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG B 2192 |
Chain | Residue |
B | ASP161 |
B | IMP2210 |
B | HOH2253 |
B | HOH2258 |
B | HOH2278 |
B | HOH2283 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG A 1191 |
Chain | Residue |
A | GLU101 |
A | ASP102 |
A | HOH1251 |
A | HOH1269 |
A | HOH1270 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG A 1192 |
Chain | Residue |
A | ASP161 |
A | IMP1210 |
A | HOH1236 |
A | HOH1257 |
A | HOH1260 |
A | HOH1274 |
site_id | AC7 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE IMP A 1210 |
Chain | Residue |
A | LEU44 |
A | LYS45 |
A | GLY46 |
A | LYS133 |
A | PHE154 |
A | VAL155 |
A | ASP161 |
A | ARG167 |
A | MG1192 |
A | HOH1257 |
A | HOH1274 |
A | HOH1283 |
A | HOH1284 |
site_id | AC8 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE IMP B 2210 |
Chain | Residue |
B | LYS45 |
B | GLY46 |
B | ASP105 |
B | LYS133 |
B | PHE154 |
B | VAL155 |
B | ASP161 |
B | ARG167 |
B | MG2192 |
B | HOH2250 |
B | HOH2253 |
B | HOH2278 |
B | HOH2283 |
B | HOH2285 |
B | HOH2291 |
Functional Information from PROSITE/UniProt
site_id | PS00103 |
Number of Residues | 13 |
Details | PUR_PYR_PR_TRANSFER Purine/pyrimidine phosphoribosyl transferases signature. VLIVEDIIDSGlT |
Chain | Residue | Details |
A | VAL97-THR109 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1a95 |
Chain | Residue | Details |
A | ASP102 | |
A | LYS133 | |
A | GLU101 | |
A | ASP105 |
site_id | CSA2 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1a95 |
Chain | Residue | Details |
B | ASP102 | |
B | LYS133 | |
B | GLU101 | |
B | ASP105 |
site_id | CSA3 |
Number of Residues | 5 |
Details | Annotated By Reference To The Literature 1a95 |
Chain | Residue | Details |
A | ASP102 | |
A | LYS133 | |
A | GLU101 | |
A | ARG137 | |
A | ASP105 |
site_id | CSA4 |
Number of Residues | 5 |
Details | Annotated By Reference To The Literature 1a95 |
Chain | Residue | Details |
B | ASP102 | |
B | LYS133 | |
B | GLU101 | |
B | ARG137 | |
B | ASP105 |