6AQS
Crystal structure of Plasmodium falciparum purine nucleoside phosphorylase (V181D) mutant complexed with DADMe-ImmG and phosphate
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 | 8 |
| Details | binding site for residue PO4 A 301 |
| Chain | Residue |
| A | GLY23 |
| A | ARG27 |
| A | ARG45 |
| A | ARG88 |
| A | GLY90 |
| A | SER91 |
| A | IM5302 |
| A | HOH410 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | binding site for residue IM5 A 302 |
| Chain | Residue |
| A | SER91 |
| A | TYR160 |
| A | ASP181 |
| A | GLU182 |
| A | MET183 |
| A | GLU184 |
| A | ASP206 |
| A | PO4301 |
| A | HOH437 |
| A | HOH476 |
| A | HOH477 |
| A | HIS7 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 303 |
| Chain | Residue |
| A | HIS119 |
| A | GLY124 |
| A | EDO304 |
| A | HOH403 |
| A | HOH406 |
| A | HOH430 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 304 |
| Chain | Residue |
| A | ARG116 |
| A | EDO303 |
| A | HOH412 |
| A | HOH487 |
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 | 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 |
