1AD4
DIHYDROPTEROATE SYNTHETASE COMPLEXED WITH OH-CH2-PTERIN-PYROPHOSPHATE FROM STAPHYLOCOCCUS AUREUS
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 | 0046654 | biological_process | tetrahydrofolate biosynthetic process |
| A | 0046656 | biological_process | folic acid biosynthetic process |
| A | 0046677 | biological_process | response to antibiotic |
| 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 | 0046654 | biological_process | tetrahydrofolate biosynthetic process |
| B | 0046656 | biological_process | folic acid biosynthetic process |
| B | 0046677 | biological_process | response to antibiotic |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN B 1 |
| Chain | Residue |
| A | HOH357 |
| A | HOH372 |
| B | HIS264 |
| B | HOH416 |
| B | HOH417 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MN A 268 |
| Chain | Residue |
| A | HIS264 |
| A | HOH413 |
| B | HOH422 |
| B | HOH423 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MN A 269 |
| Chain | Residue |
| A | ASN11 |
| A | HH2271 |
| A | HOH362 |
| A | HOH407 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE K A 270 |
| Chain | Residue |
| A | VAL75 |
| A | PHE77 |
| A | VAL79 |
| A | HOH383 |
| A | HOH384 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE K B 268 |
| Chain | Residue |
| B | VAL75 |
| B | PHE77 |
| B | VAL79 |
| B | HOH399 |
| site_id | AC6 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE HH2 A 271 |
| Chain | Residue |
| A | ASN11 |
| A | ARG52 |
| A | ASP84 |
| A | ASN103 |
| A | GLN105 |
| A | VAL126 |
| A | MET128 |
| A | ASP167 |
| A | PHE172 |
| A | ALA199 |
| A | LYS203 |
| A | ARG239 |
| A | HIS241 |
| A | MN269 |
| A | HOH325 |
| A | HOH336 |
| A | HOH362 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"9149138","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 13 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"9149138","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1AD4","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1aj0 |
| Chain | Residue | Details |
| A | ARG52 | |
| A | ASN11 | |
| A | ARG239 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1aj0 |
| Chain | Residue | Details |
| B | ASN11 | |
| B | ARG239 |
