1AD1
DIHYDROPTEROATE SYNTHETASE (APO FORM) FROM STAPHYLOCOCCUS AUREUS
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004156 | molecular_function | dihydropteroate synthase activity |
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 | 0044237 | biological_process | cellular 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 | 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 | 0044237 | biological_process | cellular 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 | 4 |
Details | BINDING SITE FOR RESIDUE K B 1 |
Chain | Residue |
B | VAL75 |
B | PHE77 |
B | VAL79 |
B | HOH291 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE K A 268 |
Chain | Residue |
A | VAL75 |
A | PHE77 |
A | VAL79 |
A | HOH517 |
A | HOH589 |
site_id | AC3 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE TRS A 500 |
Chain | Residue |
A | LYS96 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000305|PubMed:9149138 |
Chain | Residue | Details |
A | ASN11 | |
B | ASN11 |
site_id | SWS_FT_FI2 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000305|PubMed:9149138, ECO:0007744|PDB:1AD4 |
Chain | Residue | Details |
A | ARG52 | |
B | ASP167 | |
B | LYS203 | |
B | ARG239 | |
A | ASP84 | |
A | ASN103 | |
A | ASP167 | |
A | LYS203 | |
A | ARG239 | |
B | ARG52 | |
B | ASP84 | |
B | ASN103 |
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 |