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 |