3H26
Structural Studies of Pterin-Based Inhibitors of Dihydropteroate Synthase
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004156 | molecular_function | dihydropteroate synthase activity |
A | 0005829 | cellular_component | cytosol |
A | 0009396 | biological_process | folic acid-containing compound biosynthetic process |
A | 0016740 | molecular_function | transferase activity |
A | 0042558 | biological_process | pteridine-containing compound metabolic process |
A | 0044237 | biological_process | cellular metabolic process |
A | 0046654 | biological_process | tetrahydrofolate biosynthetic process |
A | 0046656 | biological_process | folic acid biosynthetic process |
A | 0046872 | molecular_function | metal ion binding |
B | 0004156 | molecular_function | dihydropteroate synthase activity |
B | 0005829 | cellular_component | cytosol |
B | 0009396 | biological_process | folic acid-containing compound biosynthetic process |
B | 0016740 | molecular_function | transferase activity |
B | 0042558 | biological_process | pteridine-containing compound metabolic process |
B | 0044237 | biological_process | cellular metabolic process |
B | 0046654 | biological_process | tetrahydrofolate biosynthetic process |
B | 0046656 | biological_process | folic acid biosynthetic process |
B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE B56 A 901 |
Chain | Residue |
A | ASP101 |
A | SO4278 |
A | HOH300 |
A | ASN120 |
A | ILE122 |
A | MET145 |
A | ASP184 |
A | PHE189 |
A | GLY216 |
A | LYS220 |
A | ARG254 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 278 |
Chain | Residue |
A | ILE25 |
A | ARG254 |
A | HIS256 |
A | HOH324 |
A | B56901 |
site_id | AC3 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 A 279 |
Chain | Residue |
A | LEU229 |
A | ARG263 |
site_id | AC4 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 A 280 |
Chain | Residue |
A | LYS50 |
A | ARG53 |
site_id | AC5 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE B56 B 902 |
Chain | Residue |
B | ASP101 |
B | ASN120 |
B | ILE122 |
B | MET145 |
B | ASP184 |
B | PHE189 |
B | LEU214 |
B | GLY216 |
B | LYS220 |
B | ARG254 |
B | SO4278 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 B 278 |
Chain | Residue |
B | ILE25 |
B | ARG254 |
B | HIS256 |
B | B56902 |
site_id | AC7 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 B 279 |
Chain | Residue |
B | LYS50 |
B | ARG53 |
site_id | AC8 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 B 280 |
Chain | Residue |
B | SER221 |
B | ARG234 |
Functional Information from PROSITE/UniProt
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1aj0 |
Chain | Residue | Details |
A | ARG254 | |
A | ASN27 |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1aj0 |
Chain | Residue | Details |
B | ARG254 | |
B | ASN27 |