3MCN
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 | 2 |
Details | BINDING SITE FOR RESIDUE MG A 423 |
Chain | Residue |
A | ASP101 |
A | ASP103 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE B57 B 423 |
Chain | Residue |
B | ASP255 |
B | ASN277 |
B | ILE301 |
B | ASP346 |
B | LYS383 |
B | ARG418 |
site_id | AC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE B57 B 424 |
Chain | Residue |
B | PHE59 |
B | ASN61 |
B | ASP101 |
B | PHE129 |
B | MG425 |
B | HOH496 |
B | GLY9 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG B 425 |
Chain | Residue |
B | GLY7 |
B | ASP101 |
B | ASP103 |
B | B57424 |
B | HOH460 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MG B 426 |
Chain | Residue |
B | GLU83 |
B | ASP101 |
B | LEU102 |
B | ASP103 |
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 |