5U0V
E. coli dihydropteroate synthase complexed with 6-methylamino-5-nitrosoisocytosine
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 | 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 | 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 | 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 | 11 |
Details | binding site for residue 7VJ A 301 |
Chain | Residue |
A | ASP96 |
A | ARG255 |
A | HOH423 |
A | ASN115 |
A | ILE117 |
A | MET139 |
A | ASP185 |
A | PHE190 |
A | LEU215 |
A | GLY217 |
A | LYS221 |
site_id | AC2 |
Number of Residues | 4 |
Details | binding site for residue NA A 302 |
Chain | Residue |
A | ASP258 |
A | HOH442 |
A | HOH498 |
A | HOH590 |
site_id | AC3 |
Number of Residues | 7 |
Details | binding site for residue ACY B 301 |
Chain | Residue |
B | LEU46 |
B | HIS257 |
B | VAL259 |
B | LYS260 |
B | HOH412 |
B | HOH418 |
B | HOH421 |
site_id | AC4 |
Number of Residues | 10 |
Details | binding site for residue 7VJ B 302 |
Chain | Residue |
B | ASP96 |
B | ASN115 |
B | MET139 |
B | ASP185 |
B | PHE190 |
B | LEU215 |
B | GLY217 |
B | LYS221 |
B | ARG255 |
B | HOH426 |
site_id | AC5 |
Number of Residues | 4 |
Details | binding site for residue NA B 303 |
Chain | Residue |
B | ASP258 |
B | HOH421 |
B | HOH491 |
B | HOH538 |
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 | ASN22 | |
B | ASN22 |
site_id | SWS_FT_FI2 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000305|PubMed:9187658, ECO:0007744|PDB:1AJ2 |
Chain | Residue | Details |
A | THR62 | |
B | ASP185 | |
B | LYS221 | |
B | ARG255 | |
A | ASP96 | |
A | ASN115 | |
A | ASP185 | |
A | LYS221 | |
A | ARG255 | |
B | THR62 | |
B | ASP96 | |
B | ASN115 |