4HB7
The Structure of Dihydropteroate Synthase from Staphylococcus aureus subsp. aureus Mu50.
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 | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 301 |
| Chain | Residue |
| A | MET232 |
| A | LYS233 |
| B | MET232 |
| B | LYS233 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 302 |
| Chain | Residue |
| A | PRO138 |
| A | GLU141 |
| A | ARG185 |
| A | HOH432 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO A 303 |
| Chain | Residue |
| A | ALA107 |
| A | LEU109 |
| A | MET128 |
| A | HIS129 |
| A | ASN130 |
| A | SER146 |
| A | TRP106 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 304 |
| Chain | Residue |
| A | LEU109 |
| A | EDO305 |
| A | EDO306 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO A 305 |
| Chain | Residue |
| A | EDO304 |
| A | EDO306 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 306 |
| Chain | Residue |
| A | TRP106 |
| A | ASN132 |
| A | EDO304 |
| A | EDO305 |
| A | HOH473 |
| A | HOH474 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO B 301 |
| Chain | Residue |
| B | TRP106 |
| B | GLY131 |
| B | ASN132 |
| B | HOH459 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P9WND1 |
| Chain | Residue | Details |
| A | ASN11 | |
| B | ASN11 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P0AC13 |
| Chain | Residue | Details |
| A | THR51 | |
| B | ASP167 | |
| B | LYS203 | |
| B | ARG239 | |
| A | ASP84 | |
| A | ASN103 | |
| A | ASP167 | |
| A | LYS203 | |
| A | ARG239 | |
| B | THR51 | |
| B | ASP84 | |
| B | ASN103 |
