5U10
E. coli dihydropteroate synthase complexed with pteroic 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 | 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 | 6 |
Details | binding site for residue PO4 A 301 |
Chain | Residue |
A | ILE20 |
A | ARG63 |
A | ARG255 |
A | HIS257 |
A | PT1302 |
A | HOH455 |
site_id | AC2 |
Number of Residues | 16 |
Details | binding site for residue PT1 A 302 |
Chain | Residue |
A | MET139 |
A | ASP185 |
A | PHE190 |
A | LEU215 |
A | GLY217 |
A | LYS221 |
A | SER222 |
A | ARG255 |
A | PO4301 |
A | HOH411 |
A | HOH425 |
A | HOH457 |
B | GLU90 |
A | THR62 |
A | ASP96 |
A | ASN115 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue PO4 B 301 |
Chain | Residue |
B | ARG255 |
B | HIS257 |
B | PT1302 |
B | HOH429 |
site_id | AC4 |
Number of Residues | 13 |
Details | binding site for residue PT1 B 302 |
Chain | Residue |
B | THR62 |
B | PRO64 |
B | ASN115 |
B | MET139 |
B | ASP185 |
B | GLY189 |
B | PHE190 |
B | GLY217 |
B | LYS221 |
B | SER222 |
B | ARG255 |
B | PO4301 |
B | HOH415 |
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 |