6JWS
Crystal structure of Plasmodium falciparum HPPK-DHPS A437G with Pteroate
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 | 0005740 | cellular_component | mitochondrial envelope |
| A | 0009396 | biological_process | folic acid-containing compound biosynthetic process |
| A | 0016301 | molecular_function | kinase activity |
| A | 0016310 | biological_process | phosphorylation |
| 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 | 0005740 | cellular_component | mitochondrial envelope |
| B | 0009396 | biological_process | folic acid-containing compound biosynthetic process |
| B | 0016301 | molecular_function | kinase activity |
| B | 0016310 | biological_process | phosphorylation |
| 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 | 18 |
| Details | binding site for residue PT1 A 801 |
| Chain | Residue |
| A | SER436 |
| A | PHE580 |
| A | PHE603 |
| A | GLY605 |
| A | LYS609 |
| A | ARG610 |
| A | ARG686 |
| A | HOH902 |
| A | HOH958 |
| A | HOH1042 |
| A | GLY437 |
| A | PRO438 |
| A | ASP482 |
| A | ASN502 |
| A | ILE504 |
| A | MET529 |
| A | ASP575 |
| A | GLY579 |
| site_id | AC2 |
| Number of Residues | 16 |
| Details | binding site for residue ATP A 802 |
| Chain | Residue |
| A | LEU181 |
| A | LYS185 |
| A | ASP208 |
| A | ASP210 |
| A | ILE211 |
| A | ASN312 |
| A | ILE313 |
| A | GLU314 |
| A | PHE315 |
| A | LEU316 |
| A | SER317 |
| A | ILE318 |
| A | HIS320 |
| A | MG803 |
| A | HOH913 |
| A | HOH954 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue MG A 803 |
| Chain | Residue |
| A | ASP208 |
| A | ASP210 |
| A | ATP802 |
| A | HOH913 |
| A | HOH954 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue CA A 804 |
| Chain | Residue |
| A | GLU42 |
| A | GLY46 |
| A | GLU99 |
| A | HOH1077 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue ACT A 805 |
| Chain | Residue |
| A | HIS530 |
| A | ARG532 |
| A | ASP550 |
| A | TYR554 |
| A | HOH992 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue ACT A 806 |
| Chain | Residue |
| A | GLN586 |
| A | LYS589 |
| A | HOH935 |
| A | HOH1018 |
| site_id | AC7 |
| Number of Residues | 18 |
| Details | binding site for residue PT1 B 801 |
| Chain | Residue |
| B | SER436 |
| B | GLY437 |
| B | PRO438 |
| B | ASP482 |
| B | ASN502 |
| B | ILE504 |
| B | MET529 |
| B | ASP575 |
| B | GLY579 |
| B | PHE580 |
| B | PHE603 |
| B | GLY605 |
| B | LYS609 |
| B | ARG610 |
| B | ARG686 |
| B | HOH933 |
| B | HOH939 |
| B | HOH1015 |
| site_id | AC8 |
| Number of Residues | 15 |
| Details | binding site for residue ATP B 802 |
| Chain | Residue |
| B | LEU181 |
| B | ASP208 |
| B | ASP210 |
| B | ILE211 |
| B | ASN312 |
| B | ILE313 |
| B | GLU314 |
| B | PHE315 |
| B | LEU316 |
| B | SER317 |
| B | HIS320 |
| B | MG803 |
| B | HOH907 |
| B | HOH942 |
| B | HOH1085 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue MG B 803 |
| Chain | Residue |
| B | ASP208 |
| B | ASP210 |
| B | ATP802 |
| B | HOH942 |
| site_id | AD1 |
| Number of Residues | 5 |
| Details | binding site for residue CA B 804 |
| Chain | Residue |
| B | GLU42 |
| B | GLY46 |
| B | GLU99 |
| B | HOH1024 |
| B | HOH1118 |
| site_id | AD2 |
| Number of Residues | 5 |
| Details | binding site for residue ACT B 805 |
| Chain | Residue |
| A | ASN510 |
| B | HIS530 |
| B | ARG532 |
| B | HOH983 |
| B | HOH1011 |
| site_id | AD3 |
| Number of Residues | 3 |
| Details | binding site for residue ACT B 806 |
| Chain | Residue |
| B | GLN586 |
| B | HOH1043 |
| B | HOH1046 |
| site_id | AD4 |
| Number of Residues | 5 |
| Details | binding site for residue MG B 807 |
| Chain | Residue |
| B | MET648 |
| B | ASP689 |
| B | GLU692 |
| B | HOH910 |
| B | HOH1044 |
Functional Information from PROSITE/UniProt
| site_id | PS00793 |
| Number of Residues | 14 |
| Details | DHPS_2 Dihydropteroate synthase signature 2. GAsVIDIGGesSgP |
| Chain | Residue | Details |
| A | GLY425-PRO438 |
