5U13
E. coli dihydropteroate synthase complexed with an 8-mercaptoguanine derivative: 2-amino-8-{[2-(4-methoxyphenyl)-2-oxoethyl]sulfanyl}-1,7-dihydro-6H-purin-6-one
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 | 14 |
Details | binding site for residue YH5 A 301 |
Chain | Residue |
A | THR62 |
A | HIS257 |
A | HOH405 |
A | HOH408 |
A | HOH434 |
B | GLU90 |
A | ASN115 |
A | MET139 |
A | ASP185 |
A | PHE190 |
A | GLY217 |
A | ARG220 |
A | LYS221 |
A | ARG255 |
site_id | AC2 |
Number of Residues | 13 |
Details | binding site for residue YH5 B 301 |
Chain | Residue |
B | ASN115 |
B | MET139 |
B | ASP185 |
B | PHE190 |
B | LEU215 |
B | GLY217 |
B | ARG220 |
B | LYS221 |
B | ARG235 |
B | ARG255 |
B | HOH421 |
B | HOH442 |
B | HOH471 |
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 |