1G9S
CRYSTAL STRUCTURE OF A COMPLEX BETWEEN E.COLI HPRT AND IMP
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 | 15 |
| Details | BINDING SITE FOR RESIDUE IMP A 190 |
| Chain | Residue |
| A | GLU103 |
| A | LEU112 |
| A | LYS135 |
| A | PHE156 |
| A | VAL157 |
| A | HOH1001 |
| A | HOH1011 |
| A | ASP104 |
| A | ILE105 |
| A | ILE106 |
| A | ASP107 |
| A | SER108 |
| A | GLY109 |
| A | ASN110 |
| A | THR111 |
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 | ASP407 |
| 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 | ARG347 | |
| B | GLY348 | |
| B | ARG469 |
| 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 | GLU403 | |
| B | ASP404 |
| 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 | ASP407 | |
| B | LYS435 |
| 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 | ASP463 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1a95 |
| Chain | Residue | Details |
| A | GLU103 | |
| A | ASP107 | |
| A | LYS135 | |
| A | ASP104 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1a95 |
| Chain | Residue | Details |
| B | GLU403 | |
| B | LYS435 | |
| B | ASP404 | |
| B | ASP407 |
| site_id | CSA3 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1a95 |
| Chain | Residue | Details |
| A | GLU103 | |
| A | ASP107 | |
| A | LYS135 | |
| A | ASP104 | |
| A | ARG139 |
| site_id | CSA4 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1a95 |
| Chain | Residue | Details |
| B | GLU403 | |
| B | LYS435 | |
| B | ASP404 | |
| B | ASP407 | |
| B | ARG439 |
