Structure of PDB 6jwt Chain A Binding Site BS01

Receptor Information
>6jwt Chain A (length=548) Species: 5833 (Plasmodium falciparum) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
LILSEENKTNIAVLNLGTNDRRNAVLILETALHLVEKYLGKIINTSYLYE
TVPVNYINELMQNLEESKYEENKELIDKCEEYETFLKNGKVDNSILKEVN
VENYLLECNNIIVKNDESYFYNLTVVVKTFVNDPLSMLVVIKYIEELMKI
IDIDILFFNDFTIFMKNIKLEKNMIYKILSKYIHLERFRDPQEIINNMVD
NIEFLSIPHVYTTHRYSILLCLNDMIPEYKHNVLNNTIRCLYNKYVSRMK
EQYNINIKENNKRIYVLKDRISYLKEKTNIVGILNVNVEPKRAVQRMFEM
INEGASVIDIGGESFGPFVIPNPKISERDLVVPVLQLFQKEWNDIKNKIV
KCDAKPIISIDTINYNVFKECVDNDLVDILNDISACTNNPEIIKLLKKKN
KFYSVVLMHKRGNPHTMDKLTNYDNLVYDIKNYLEQRLNFLVLNGIPRYR
ILFDIGLGFAKKHDQSIKLLQNIHVYDEYPLFIGYSRKRFITHCMNDKDQ
LLYQKNICGGLAIASYSYYKKVDLIRVHDVLETKSVLDVLTKIDQVKD
Ligand information
Ligand IDAMP
InChIInChI=1S/C10H14N5O7P/c11-8-5-9(13-2-12-8)15(3-14-5)10-7(17)6(16)4(22-10)1-21-23(18,19)20/h2-4,6-7,10,16-17H,1H2,(H2,11,12,13)(H2,18,19,20)/t4-,6-,7-,10-/m1/s1
InChIKeyUDMBCSSLTHHNCD-KQYNXXCUSA-N
SMILES
SoftwareSMILES
CACTVS 3.370Nc1ncnc2n(cnc12)[CH]3O[CH](CO[P](O)(O)=O)[CH](O)[CH]3O
CACTVS 3.370Nc1ncnc2n(cnc12)[C@@H]3O[C@H](CO[P](O)(O)=O)[C@@H](O)[C@H]3O
OpenEye OEToolkits 1.7.6c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)COP(=O)(O)O)O)O)N
ACDLabs 12.01O=P(O)(O)OCC3OC(n2cnc1c(ncnc12)N)C(O)C3O
OpenEye OEToolkits 1.7.6c1nc(c2c(n1)n(cn2)C3C(C(C(O3)COP(=O)(O)O)O)O)N
FormulaC10 H14 N5 O7 P
NameADENOSINE MONOPHOSPHATE
ChEMBLCHEMBL752
DrugBankDB00131
ZINCZINC000003860156
PDB chain6jwt Chain A Residue 801 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB6jwt The structure of Plasmodium falciparum hydroxymethyldihydropterin pyrophosphokinase-dihydropteroate synthase reveals the basis of sulfa resistance.
Resolution2.56 Å
Binding residue
(original residue number in PDB)		L181 D210 I211 N312 F315 L316 S317 H320
Binding residue
(residue number reindexed from 1)		L138 D154 I155 N201 F204 L205 S206 H209
Annotation score5
Enzymatic activity
Enzyme Commision number 2.5.1.15: dihydropteroate synthase.
2.7.6.3: 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase.
Gene Ontology
Molecular Function
GO:0003848 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase activity
GO:0004156 dihydropteroate synthase activity
GO:0005524 ATP binding
GO:0016301 kinase activity
GO:0046872 metal ion binding
Biological Process
GO:0009396 folic acid-containing compound biosynthetic process
GO:0016310 phosphorylation
GO:0042558 pteridine-containing compound metabolic process
GO:0044237 cellular metabolic process
GO:0046654 tetrahydrofolate biosynthetic process
GO:0046656 folic acid biosynthetic process
Cellular Component
GO:0005740 mitochondrial envelope

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:6jwt, PDBe:6jwt, PDBj:6jwt
PDBsum6jwt
PubMed31883412
UniProtQ25704

[Back to BioLiP]