2BSX
Crystal structure of the Plasmodium falciparum purine nucleoside phosphorylase complexed with inosine
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004731 | molecular_function | purine-nucleoside phosphorylase activity |
| A | 0004850 | molecular_function | uridine phosphorylase activity |
| A | 0005829 | cellular_component | cytosol |
| A | 0006148 | biological_process | inosine catabolic process |
| A | 0006166 | biological_process | purine ribonucleoside salvage |
| A | 0006195 | biological_process | purine nucleotide catabolic process |
| A | 0006218 | biological_process | uridine catabolic process |
| A | 0009116 | biological_process | nucleoside metabolic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016757 | molecular_function | glycosyltransferase activity |
| A | 0017061 | molecular_function | S-methyl-5-thioadenosine phosphorylase activity |
| A | 0047975 | molecular_function | guanosine phosphorylase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE NOS A1248 |
| Chain | Residue |
| A | HIS7 |
| A | TRP212 |
| A | ARG45 |
| A | SER91 |
| A | CYS92 |
| A | GLY93 |
| A | TYR160 |
| A | MET183 |
| A | GLU184 |
| A | ASP206 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"UniProtKB","id":"Q8I3X4","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q8I3X4","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"30602534","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5ZNI","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | Binding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"30602534","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5ZNC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5ZNI","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Binding site: {"description":"in other chain","evidences":[{"source":"UniProtKB","id":"Q8I3X4","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | a catalytic site defined by CSA, PubMed 16131758 |
| Chain | Residue | Details |
| A | ASP206 |
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 695 |
| Chain | Residue | Details |
| A | ARG27 | electrostatic stabiliser |
| A | ARG45 | electrostatic stabiliser |
| A | ARG88 | electrostatic stabiliser |
| A | ASP206 | proton acceptor, proton donor |
