1AD4
DIHYDROPTEROATE SYNTHETASE COMPLEXED WITH OH-CH2-PTERIN-PYROPHOSPHATE FROM STAPHYLOCOCCUS AUREUS
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004156 | molecular_function | dihydropteroate synthase activity |
A | 0005829 | cellular_component | cytosol |
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 | 0005829 | cellular_component | cytosol |
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 | 5 |
Details | BINDING SITE FOR RESIDUE MN B 1 |
Chain | Residue |
A | HOH357 |
A | HOH372 |
B | HIS264 |
B | HOH416 |
B | HOH417 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MN A 268 |
Chain | Residue |
A | HIS264 |
A | HOH413 |
B | HOH422 |
B | HOH423 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MN A 269 |
Chain | Residue |
A | ASN11 |
A | HH2271 |
A | HOH362 |
A | HOH407 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE K A 270 |
Chain | Residue |
A | VAL75 |
A | PHE77 |
A | VAL79 |
A | HOH383 |
A | HOH384 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE K B 268 |
Chain | Residue |
B | VAL75 |
B | PHE77 |
B | VAL79 |
B | HOH399 |
site_id | AC6 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE HH2 A 271 |
Chain | Residue |
A | ASN11 |
A | ARG52 |
A | ASP84 |
A | ASN103 |
A | GLN105 |
A | VAL126 |
A | MET128 |
A | ASP167 |
A | PHE172 |
A | ALA199 |
A | LYS203 |
A | ARG239 |
A | HIS241 |
A | MN269 |
A | HOH325 |
A | HOH336 |
A | HOH362 |
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 |