6JWQ
Crystal structure of Plasmodium falciparum HPPK-DHPS wild type
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 | 0005524 | molecular_function | ATP binding |
A | 0009396 | biological_process | folic acid-containing compound biosynthetic process |
A | 0016301 | molecular_function | kinase 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 | 0003848 | molecular_function | 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase activity |
B | 0004156 | molecular_function | dihydropteroate synthase activity |
B | 0005524 | molecular_function | ATP binding |
B | 0009396 | biological_process | folic acid-containing compound biosynthetic process |
B | 0016301 | molecular_function | kinase 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 | 4 |
Details | binding site for residue MG A 801 |
Chain | Residue |
A | ASP208 |
A | ASP210 |
A | ATP802 |
A | HOH922 |
site_id | AC2 |
Number of Residues | 16 |
Details | binding site for residue ATP A 802 |
Chain | Residue |
A | ASN312 |
A | ILE313 |
A | GLU314 |
A | PHE315 |
A | LEU316 |
A | SER317 |
A | ILE318 |
A | HIS320 |
A | ARG326 |
A | MG801 |
A | HOH956 |
A | LEU181 |
A | LYS185 |
A | ASP208 |
A | ASP210 |
A | ILE211 |
site_id | AC3 |
Number of Residues | 3 |
Details | binding site for residue CA A 803 |
Chain | Residue |
A | GLU42 |
A | GLY46 |
A | GLU99 |
site_id | AC4 |
Number of Residues | 5 |
Details | binding site for residue ACT A 804 |
Chain | Residue |
A | HIS530 |
A | ARG532 |
A | ASP550 |
A | TYR554 |
A | HOH920 |
site_id | AC5 |
Number of Residues | 11 |
Details | binding site for residue AMP B 801 |
Chain | Residue |
B | ASP208 |
B | ASP210 |
B | ILE211 |
B | ASN312 |
B | ILE313 |
B | GLU314 |
B | PHE315 |
B | LEU316 |
B | SER317 |
B | HIS320 |
B | MG802 |
site_id | AC6 |
Number of Residues | 4 |
Details | binding site for residue MG B 802 |
Chain | Residue |
B | ASP208 |
B | ASP210 |
B | AMP801 |
B | HOH932 |
site_id | AC7 |
Number of Residues | 5 |
Details | binding site for residue ACT B 803 |
Chain | Residue |
A | ASN510 |
A | HOH913 |
A | HOH957 |
B | HIS530 |
B | ARG532 |
Functional Information from PROSITE/UniProt
site_id | PS00793 |
Number of Residues | 14 |
Details | DHPS_2 Dihydropteroate synthase signature 2. GAsVIDIGGesSaP |
Chain | Residue | Details |
A | GLY425-PRO438 |