3TYZ
Crystal Structure of the Yersinia pestis Dihydropteroate synthetase with substrate transition state 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 | 12 |
| Details | BINDING SITE FOR RESIDUE XHP A 278 |
| Chain | Residue |
| A | ASP96 |
| A | POP279 |
| A | PAB280 |
| A | HOH352 |
| A | ASN115 |
| A | ILE117 |
| A | ASP185 |
| A | PHE190 |
| A | LEU215 |
| A | GLY217 |
| A | LYS221 |
| A | ARG255 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE POP A 279 |
| Chain | Residue |
| A | ASN22 |
| A | SER27 |
| A | PHE28 |
| A | SER61 |
| A | THR62 |
| A | ARG63 |
| A | ARG255 |
| A | HIS257 |
| A | XHP278 |
| A | PAB280 |
| A | MG281 |
| A | HOH303 |
| A | HOH307 |
| A | HOH322 |
| site_id | AC3 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE PAB A 280 |
| Chain | Residue |
| A | PHE28 |
| A | THR62 |
| A | ARG63 |
| A | PHE190 |
| A | LYS221 |
| A | SER222 |
| A | XHP278 |
| A | POP279 |
| A | HOH289 |
| A | HOH290 |
| A | HOH320 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 281 |
| Chain | Residue |
| A | ASN22 |
| A | SER27 |
| A | POP279 |
| A | HOH305 |
| A | HOH306 |
| A | HOH307 |
| site_id | AC5 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE XHP B 278 |
| Chain | Residue |
| B | ASP96 |
| B | ASN115 |
| B | ILE117 |
| B | MET139 |
| B | ASP185 |
| B | PHE190 |
| B | LEU215 |
| B | GLY217 |
| B | LYS221 |
| B | ARG255 |
| B | POP279 |
| B | PAB280 |
| B | HOH283 |
| B | HOH295 |
| site_id | AC6 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE POP B 279 |
| Chain | Residue |
| B | ASN22 |
| B | SER27 |
| B | PHE28 |
| B | SER61 |
| B | THR62 |
| B | ARG63 |
| B | ARG255 |
| B | HIS257 |
| B | XHP278 |
| B | PAB280 |
| B | MG281 |
| B | HOH283 |
| B | HOH287 |
| B | HOH303 |
| site_id | AC7 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE PAB B 280 |
| Chain | Residue |
| B | PHE28 |
| B | THR62 |
| B | ARG63 |
| B | GLY189 |
| B | PHE190 |
| B | LYS221 |
| B | SER222 |
| B | XHP278 |
| B | POP279 |
| B | HOH292 |
| B | HOH293 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 281 |
| Chain | Residue |
| B | ASN22 |
| B | POP279 |
| B | HOH282 |
| B | HOH283 |
| B | HOH284 |
Functional Information from PROSITE/UniProt
