3H2E
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 | 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 | 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 | 7 |
Details | BINDING SITE FOR RESIDUE SO4 A 278 |
Chain | Residue |
A | ASN27 |
A | ARG68 |
A | PRO69 |
A | ARG254 |
A | HIS256 |
A | HOH295 |
A | HOH395 |
site_id | AC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 A 279 |
Chain | Residue |
A | HOH331 |
A | LYS50 |
A | ARG53 |
site_id | AC3 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE SO4 A 280 |
Chain | Residue |
A | ARG219 |
site_id | AC4 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 A 281 |
Chain | Residue |
A | SER221 |
A | ARG234 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE B59 B 901 |
Chain | Residue |
A | PHE33 |
B | LYS81 |
B | LYS109 |
B | HIS137 |
B | TYR138 |
B | B59902 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE B59 B 902 |
Chain | Residue |
B | LYS81 |
B | GLN88 |
B | LYS109 |
B | GLN110 |
B | HOH391 |
B | B59901 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 B 278 |
Chain | Residue |
B | ARG254 |
B | HIS256 |
B | HOH360 |
B | HOH368 |
site_id | AC8 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 B 279 |
Chain | Residue |
B | ASN27 |
B | ARG219 |
site_id | AC9 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 B 280 |
Chain | Residue |
B | LYS50 |
B | ARG53 |
site_id | BC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 B 281 |
Chain | Residue |
B | SER221 |
B | ARG234 |
B | HOH400 |
Functional Information from PROSITE/UniProt
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1aj0 |
Chain | Residue | Details |
A | ARG254 | |
A | ARG68 | |
A | ASN27 |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1aj0 |
Chain | Residue | Details |
B | ARG254 | |
B | ASN27 |