3MCO
Crystal Structure of the 6-hyroxymethyl-7,8-dihydropterin pyrophosphokinase dihydropteroate synthase bifunctional enzyme from Francisella tularensis
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003848 | molecular_function | 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase activity |
| A | 0004156 | molecular_function | dihydropteroate synthase activity |
| A | 0009396 | biological_process | folic acid-containing compound biosynthetic process |
| A | 0042558 | biological_process | pteridine-containing compound metabolic process |
| B | 0003848 | molecular_function | 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase activity |
| B | 0004156 | molecular_function | dihydropteroate synthase activity |
| B | 0009396 | biological_process | folic acid-containing compound biosynthetic process |
| B | 0042558 | biological_process | pteridine-containing compound metabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PH2 A 423 |
| Chain | Residue |
| A | SER43 |
| A | MG427 |
| A | LYS44 |
| A | VAL46 |
| A | PHE59 |
| A | ASN61 |
| A | TRP95 |
| A | ASP101 |
| A | PHE129 |
| A | APC425 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PH2 A 424 |
| Chain | Residue |
| A | THR216 |
| A | ASP255 |
| A | ASN277 |
| A | ILE301 |
| A | ASP346 |
| A | PHE349 |
| A | LEU377 |
| A | LYS383 |
| A | ARG418 |
| site_id | AC3 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE APC A 425 |
| Chain | Residue |
| A | LEU76 |
| A | LYS80 |
| A | ARG88 |
| A | TRP95 |
| A | ARG98 |
| A | ASP101 |
| A | ASP103 |
| A | ILE104 |
| A | LYS116 |
| A | LEU117 |
| A | THR118 |
| A | HIS121 |
| A | ARG127 |
| A | PH2423 |
| A | MG426 |
| A | MG427 |
| A | HOH453 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 426 |
| Chain | Residue |
| A | ASP101 |
| A | ASP103 |
| A | APC425 |
| A | MG427 |
| A | HOH456 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 427 |
| Chain | Residue |
| A | ASP101 |
| A | ASP103 |
| A | PH2423 |
| A | APC425 |
| A | MG426 |
| site_id | AC6 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PH2 B 423 |
| Chain | Residue |
| B | SER43 |
| B | LYS44 |
| B | VAL46 |
| B | PHE59 |
| B | ASN61 |
| B | ARG98 |
| B | ASP101 |
| B | PHE129 |
| B | APC425 |
| B | MG427 |
| site_id | AC7 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PH2 B 424 |
| Chain | Residue |
| B | ASP255 |
| B | ASN277 |
| B | VAL279 |
| B | ILE301 |
| B | ASP346 |
| B | PHE349 |
| B | PHE351 |
| B | GLY379 |
| B | LYS383 |
| B | ARG418 |
| site_id | AC8 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE APC B 425 |
| Chain | Residue |
| B | LEU76 |
| B | LYS80 |
| B | ARG98 |
| B | ASP101 |
| B | ASP103 |
| B | ILE104 |
| B | LYS116 |
| B | LEU117 |
| B | THR118 |
| B | HIS121 |
| B | ARG127 |
| B | PH2423 |
| B | MG426 |
| B | MG427 |
| B | HOH444 |
| B | HOH450 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG B 426 |
| Chain | Residue |
| B | ASP101 |
| B | ASP103 |
| B | APC425 |
| B | HOH438 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 427 |
| Chain | Residue |
| B | ASP101 |
| B | ASP103 |
| B | ARG127 |
| B | PH2423 |
| B | APC425 |
Functional Information from PROSITE/UniProt
| site_id | PS00793 |
| Number of Residues | 14 |
| Details | DHPS_2 Dihydropteroate synthase signature 2. GAeIIDIGAesTkP |
| Chain | Residue | Details |
| A | GLY205-PRO218 |
