3TYD
Dihydropteroate Synthase in complex with PPi and DHP+
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 | 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 | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE POP A 701 |
| Chain | Residue |
| A | ILE25 |
| A | ASN27 |
| A | SER66 |
| A | ARG254 |
| A | HIS256 |
| A | XHP801 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE XHP A 801 |
| Chain | Residue |
| A | MET145 |
| A | ASP184 |
| A | PHE189 |
| A | GLY216 |
| A | LYS220 |
| A | ARG254 |
| A | POP701 |
| A | ASP101 |
| A | ASN120 |
| A | ILE122 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 A 278 |
| Chain | Residue |
| A | LYS19 |
| A | LYS266 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 A 279 |
| Chain | Residue |
| A | LYS50 |
| A | ARG53 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 280 |
| Chain | Residue |
| A | GLU198 |
| A | ARG201 |
| A | ASN202 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 A 281 |
| Chain | Residue |
| A | ARG219 |
| A | HOH297 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 A 282 |
| Chain | Residue |
| A | SER221 |
| A | ARG234 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 283 |
| Chain | Residue |
| A | LYS109 |
| A | HIS137 |
| A | HOH291 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE POP B 702 |
| Chain | Residue |
| B | ILE25 |
| B | ASN27 |
| B | SER66 |
| B | ARG254 |
| B | HIS256 |
| B | XHP802 |
| site_id | BC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE XHP B 802 |
| Chain | Residue |
| B | ASP101 |
| B | ASN120 |
| B | ILE122 |
| B | ASP184 |
| B | PHE189 |
| B | LEU214 |
| B | GLY216 |
| B | LYS220 |
| B | ARG254 |
| B | POP702 |
| site_id | BC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 B 278 |
| Chain | Residue |
| B | ARG219 |
| B | HOH286 |
| site_id | BC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 B 279 |
| Chain | Residue |
| B | LYS50 |
| B | ARG53 |
| site_id | BC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 B 280 |
| Chain | Residue |
| B | SER221 |
| B | ARG234 |
| site_id | BC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 B 281 |
| Chain | Residue |
| B | ARG201 |
| B | ASN202 |
| site_id | BC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 B 282 |
| Chain | Residue |
| B | LYS19 |
| B | LYS266 |
| site_id | BC7 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE SO4 B 283 |
| Chain | Residue |
| B | ARG8 |
Functional Information from PROSITE/UniProt
