1J7J
Crystal Structure of the HPRT from Salmonella typhimurium
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 | 0006177 | biological_process | GMP biosynthetic process |
| A | 0006178 | biological_process | guanine salvage |
| A | 0006188 | biological_process | IMP biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016757 | molecular_function | glycosyltransferase activity |
| A | 0032263 | biological_process | GMP salvage |
| A | 0032264 | biological_process | IMP salvage |
| A | 0043101 | biological_process | purine-containing compound 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 | 0006177 | biological_process | GMP biosynthetic process |
| B | 0006178 | biological_process | guanine salvage |
| B | 0006188 | biological_process | IMP biosynthetic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016757 | molecular_function | glycosyltransferase activity |
| B | 0032263 | biological_process | GMP salvage |
| B | 0032264 | biological_process | IMP salvage |
| B | 0043101 | biological_process | purine-containing compound 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 | 2 |
| Details | BINDING SITE FOR RESIDUE MG A 600 |
| Chain | Residue |
| A | GLU99 |
| A | ASP100 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG B 601 |
| Chain | Residue |
| B | GLU99 |
| B | ASP100 |
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 | VAL95-THR107 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"P0A9M2","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P9WHQ9","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2009","submissionDatabase":"PDB data bank","title":"Crystal structure of the HPRT from Salmonella typhimurium at 2.3 A resolution.","authors":["Lee C.C.","Focia P.J.","Spraggon G.","Eakin A.E."]}},{"source":"PDB","id":"1J7J","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 14 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P0A9M2","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1a95 |
| Chain | Residue | Details |
| A | ASP103 | |
| A | ASP100 | |
| A | LYS131 | |
| A | GLU99 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1a95 |
| Chain | Residue | Details |
| B | ASP103 | |
| B | ASP100 | |
| B | LYS131 | |
| B | GLU99 |
| site_id | CSA3 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1a95 |
| Chain | Residue | Details |
| A | ASP103 | |
| A | ARG135 | |
| A | ASP100 | |
| A | LYS131 | |
| A | GLU99 |
| site_id | CSA4 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1a95 |
| Chain | Residue | Details |
| B | ASP103 | |
| B | ARG135 | |
| B | ASP100 | |
| B | LYS131 | |
| B | GLU99 |
