1SQ6
Plasmodium falciparum homolog of Uridine phosphorylase/Purine nucleoside phosphorylase
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 | 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 | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 401 |
Chain | Residue |
A | GLY31 |
A | ARG53 |
A | ARG96 |
A | GLY98 |
A | SER99 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Proton donor => ECO:0000305|PubMed:24416224 |
Chain | Residue | Details |
A | ASP214 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000305|PubMed:24416224, ECO:0000305|Ref.7, ECO:0007744|PDB:3FOW, ECO:0007744|PDB:3PHC |
Chain | Residue | Details |
A | HIS15 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | BINDING: in other chain => ECO:0000269|PubMed:24416224, ECO:0000269|Ref.7, ECO:0000305|PubMed:14982926, ECO:0000305|PubMed:19575810, ECO:0007744|PDB:1NW4, ECO:0007744|PDB:1Q1G, ECO:0007744|PDB:3ENZ, ECO:0007744|PDB:3FOW, ECO:0007744|PDB:3PHC |
Chain | Residue | Details |
A | GLY31 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:24416224, ECO:0000269|Ref.7, ECO:0000305|PubMed:14982926, ECO:0000305|PubMed:19575810, ECO:0007744|PDB:1NW4, ECO:0007744|PDB:1Q1G, ECO:0007744|PDB:3ENZ, ECO:0007744|PDB:3FOW, ECO:0007744|PDB:3PHC |
Chain | Residue | Details |
A | ARG53 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | BINDING: in other chain => ECO:0000269|PubMed:24416224, ECO:0000269|PubMed:29440412, ECO:0000269|Ref.7, ECO:0000305|PubMed:14982926, ECO:0000305|PubMed:19575810, ECO:0007744|PDB:1NW4, ECO:0007744|PDB:1Q1G, ECO:0007744|PDB:3ENZ, ECO:0007744|PDB:3FOW, ECO:0007744|PDB:3PHC, ECO:0007744|PDB:6AQS, ECO:0007744|PDB:6AQU |
Chain | Residue | Details |
A | ARG96 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | BINDING: in other chain => ECO:0000269|PubMed:16131758, ECO:0000305|PubMed:24416224, ECO:0000305|Ref.7, ECO:0007744|PDB:2BSX, ECO:0007744|PDB:3FOW, ECO:0007744|PDB:3PHC |
Chain | Residue | Details |
A | MSE191 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 4 |
Details | M-CSA 695 |
Chain | Residue | Details |
A | ARG35 | electrostatic stabiliser |
A | ARG53 | electrostatic stabiliser |
A | ARG96 | electrostatic stabiliser |
A | ASP214 | proton acceptor, proton donor |