Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004422 | molecular_function | hypoxanthine phosphoribosyltransferase activity |
| A | 0006166 | biological_process | purine ribonucleoside salvage |
| B | 0004422 | molecular_function | hypoxanthine phosphoribosyltransferase activity |
| B | 0006166 | biological_process | purine ribonucleoside salvage |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE 5GP A 1224 |
| Chain | Residue |
| A | ASP146 |
| A | LYS174 |
| A | PHE195 |
| A | VAL196 |
| A | LEU201 |
| A | ASP202 |
| A | TYR203 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1225 |
| Chain | Residue |
| A | ASP146 |
| A | THR147 |
| A | GLY148 |
| A | THR150 |
| A | LYS77 |
| A | GLU142 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE 5GP B 1227 |
| Chain | Residue |
| B | LYS77 |
| B | LYS174 |
| B | PHE195 |
| B | VAL196 |
| B | LEU201 |
| B | ASP202 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1228 |
| Chain | Residue |
| B | LYS77 |
| B | GLU142 |
| B | ILE145 |
| B | ASP146 |
| B | THR147 |
| B | GLY148 |
| B | LYS149 |
| B | THR150 |
| B | MET151 |
Functional Information from PROSITE/UniProt
| site_id | PS00103 |
| Number of Residues | 13 |
| Details | PUR_PYR_PR_TRANSFER Purine/pyrimidine phosphoribosyl transferases signature. VLIVEDIIDTGkT |
| Chain | Residue | Details |
| A | VAL138-THR150 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 20 |
| Details | Binding site: {} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"8044844","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10433693","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P27605","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]} |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P00493","evidenceCode":"ECO:0000250"}]} |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1a95 |
| Chain | Residue | Details |
| A | GLU142 | |
| A | ASP143 | |
| A | LYS174 | |
| A | ASP146 | |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1a95 |
| Chain | Residue | Details |
| B | GLU142 | |
| B | ASP143 | |
| B | LYS174 | |
| B | ASP146 | |
| site_id | CSA3 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1a95 |
| Chain | Residue | Details |
| A | GLU142 | |
| A | ASP143 | |
| A | LYS174 | |
| A | ASP146 | |
| A | LEU178 | |
| site_id | CSA4 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1a95 |
| Chain | Residue | Details |
| B | GLU142 | |
| B | ASP143 | |
| B | LYS174 | |
| B | ASP146 | |
| B | LEU178 | |
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 48 |
| Chain | Residue | Details |
| A | GLU142 | attractive charge-charge interaction, electrostatic stabiliser |
| A | ASP143 | attractive charge-charge interaction, electrostatic stabiliser |
| A | ASP146 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | PHE195 | electrostatic stabiliser |
| A | ARG208 | electrostatic stabiliser |
| site_id | MCSA2 |
| Number of Residues | 5 |
| Details | M-CSA 48 |
| Chain | Residue | Details |
| B | GLU142 | attractive charge-charge interaction, electrostatic stabiliser |
| B | ASP143 | attractive charge-charge interaction, electrostatic stabiliser |
| B | ASP146 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | PHE195 | electrostatic stabiliser |
| B | ARG208 | electrostatic stabiliser |
