3TZF
Crystal Structure of the Yersinia pestis Dihydropteroate Synthase with Sulfonamide Drug Complex.
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 | 19 |
Details | BINDING SITE FOR RESIDUE HH2 A 278 |
Chain | Residue |
A | ASN22 |
A | ASP185 |
A | PHE190 |
A | GLY217 |
A | LYS221 |
A | ARG255 |
A | HIS257 |
A | MG279 |
A | HOH280 |
A | HOH353 |
A | HOH387 |
A | SER27 |
A | PHE28 |
A | SER61 |
A | THR62 |
A | ARG63 |
A | ASP96 |
A | ASN115 |
A | ILE117 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG A 279 |
Chain | Residue |
A | ASN22 |
A | SER27 |
A | HH2278 |
A | HOH317 |
A | HOH352 |
A | HOH353 |
site_id | AC3 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE HH2 B 278 |
Chain | Residue |
B | ASN22 |
B | SER27 |
B | PHE28 |
B | SER61 |
B | THR62 |
B | ARG63 |
B | ASP96 |
B | ASN115 |
B | ILE117 |
B | MET139 |
B | ASP185 |
B | PHE190 |
B | GLY217 |
B | LYS221 |
B | ARG255 |
B | HIS257 |
B | MG279 |
B | 08D280 |
B | HOH283 |
B | HOH298 |
B | HOH299 |
B | HOH301 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG B 279 |
Chain | Residue |
B | ASN22 |
B | HH2278 |
B | HOH298 |
B | HOH299 |
B | HOH306 |
site_id | AC5 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE 08D B 280 |
Chain | Residue |
B | PHE28 |
B | THR62 |
B | ARG63 |
B | PRO64 |
B | GLY189 |
B | PHE190 |
B | LYS221 |
B | SER222 |
B | HH2278 |
B | HOH289 |
B | HOH333 |
Functional Information from PROSITE/UniProt