6APT
Trypanosoma brucei hypoxanthine guanine phosphoribosyltransferase in complex with {[(2S)-3-(2-amino-6-oxo-1,6-dihydro-9H-purin-9-yl)propane-1,2-diyl]bis(oxyethane-2,1-diyl)}bis(phosphonic acid)
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 | 0016740 | molecular_function | transferase activity |
A | 0016757 | molecular_function | glycosyltransferase activity |
A | 0020015 | cellular_component | glycosome |
A | 0031981 | cellular_component | nuclear lumen |
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 |
A | 0097014 | cellular_component | ciliary plasm |
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 | 0016740 | molecular_function | transferase activity |
B | 0016757 | molecular_function | glycosyltransferase activity |
B | 0020015 | cellular_component | glycosome |
B | 0031981 | cellular_component | nuclear lumen |
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 |
B | 0097014 | cellular_component | ciliary plasm |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 20 |
Details | binding site for residue 45T A 301 |
Chain | Residue |
A | LYS54 |
A | VAL165 |
A | PHE166 |
A | VAL167 |
A | LEU172 |
A | ASP173 |
A | ARG179 |
A | HOH402 |
A | HOH408 |
A | HOH419 |
A | HOH428 |
A | GLY55 |
A | HOH444 |
A | ILE115 |
A | ASP117 |
A | THR118 |
A | ALA119 |
A | LEU120 |
A | THR121 |
A | LYS145 |
site_id | AC2 |
Number of Residues | 9 |
Details | binding site for residue PEG A 302 |
Chain | Residue |
A | GLU17 |
A | HIS21 |
A | HIS21 |
A | ASP62 |
A | ASP62 |
A | ARG65 |
A | ILE66 |
A | ARG182 |
A | HOH430 |
site_id | AC3 |
Number of Residues | 20 |
Details | binding site for residue 45T B 301 |
Chain | Residue |
B | LYS54 |
B | GLY55 |
B | ILE115 |
B | ASP117 |
B | THR118 |
B | ALA119 |
B | LEU120 |
B | THR121 |
B | LYS145 |
B | VAL165 |
B | PHE166 |
B | VAL167 |
B | LEU172 |
B | ASP173 |
B | ARG179 |
B | HOH405 |
B | HOH420 |
B | HOH423 |
B | HOH432 |
B | HOH440 |
site_id | AC4 |
Number of Residues | 7 |
Details | binding site for residue PEG B 302 |
Chain | Residue |
B | GLU17 |
B | HIS21 |
B | HIS21 |
B | ARG65 |
B | ILE66 |
B | ARG182 |
B | HOH403 |
Functional Information from PROSITE/UniProt
site_id | PS00103 |
Number of Residues | 13 |
Details | PUR_PYR_PR_TRANSFER Purine/pyrimidine phosphoribosyl transferases signature. VLVLEDILDTAlT |
Chain | Residue | Details |
A | VAL109-THR121 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor => ECO:0000250 |
Chain | Residue | Details |
A | ASP117 | |
B | ASP117 |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | LYS54 | |
A | GLU113 | |
A | LYS145 | |
A | ASP173 | |
B | LYS54 | |
B | GLU113 | |
B | LYS145 | |
B | ASP173 |