2VEG
Dihydropteroate synthase from Streptococcus pneumoniae: complex with 6-hydroxymethyl-7,8-dihydropterin monophosphate
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 | 13 |
| Details | BINDING SITE FOR RESIDUE PMM A1304 |
| Chain | Residue |
| A | ILE15 |
| A | GLY233 |
| A | LYS237 |
| A | ARG282 |
| A | HIS284 |
| A | ASN17 |
| A | ASP91 |
| A | ASN110 |
| A | ILE112 |
| A | MET135 |
| A | ASP201 |
| A | PHE206 |
| A | PHE231 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PO4 A1305 |
| Chain | Residue |
| A | ALA44 |
| A | GLU45 |
| A | GLY46 |
| A | THR255 |
| A | GLU256 |
| A | ARG290 |
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:O05701 |
| Chain | Residue | Details |
| A | ASN17 | |
| B | ASN17 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:18321242 |
| Chain | Residue | Details |
| A | ASP91 | |
| B | ASP91 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:18321242, ECO:0007744|PDB:2VEG |
| Chain | Residue | Details |
| A | ASN110 | |
| A | ASP201 | |
| A | LYS237 | |
| A | ARG282 | |
| B | ASN110 | |
| B | ASP201 | |
| B | LYS237 | |
| B | ARG282 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1aj0 |
| Chain | Residue | Details |
| A | ASN17 | |
| A | ARG282 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1aj0 |
| Chain | Residue | Details |
| B | ASN17 | |
| B | ARG282 |
