5U0Y
E. coli dihydropteroate synthase complexed with an 8-mercaptoguanine derivative: [(2-amino-6-oxo-6,9-dihydro-1H-purin-8-yl)sulfanyl]acetic acid
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004156 | molecular_function | dihydropteroate synthase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0009396 | biological_process | folic acid-containing compound biosynthetic process |
| A | 0009410 | biological_process | response to xenobiotic stimulus |
| 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 | 0046872 | molecular_function | metal ion binding |
| B | 0004156 | molecular_function | dihydropteroate synthase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0009396 | biological_process | folic acid-containing compound biosynthetic process |
| B | 0009410 | biological_process | response to xenobiotic stimulus |
| 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 | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | binding site for residue 7PJ A 301 |
| Chain | Residue |
| A | THR62 |
| A | ARG255 |
| A | HOH438 |
| A | HOH458 |
| A | HOH510 |
| A | ASP96 |
| A | ASN115 |
| A | MET139 |
| A | ASP185 |
| A | PHE190 |
| A | LEU215 |
| A | GLY217 |
| A | LYS221 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 302 |
| Chain | Residue |
| A | SER233 |
| A | GLU234 |
| A | ARG235 |
| A | LEU236 |
| A | SER237 |
| B | GLU264 |
| site_id | AC3 |
| Number of Residues | 13 |
| Details | binding site for residue 7PJ B 301 |
| Chain | Residue |
| B | ASN115 |
| B | MET139 |
| B | ASP185 |
| B | PHE190 |
| B | GLY217 |
| B | LYS221 |
| B | ARG255 |
| B | HOH408 |
| B | HOH421 |
| B | HOH423 |
| B | HOH429 |
| B | HOH438 |
| B | HOH501 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P9WND1","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 14 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P0AC13","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"37419898","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7TQ1","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
