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 |
A | 0044237 | biological_process | cellular 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 |
B | 0044237 | biological_process | cellular 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 |