Structure of PDB 6jwq Chain B Binding Site BS01

Receptor Information
>6jwq Chain B (length=590) Species: 5833 (Plasmodium falciparum) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
ELILSEENKTNIAVLNLGTNDRRNAVLILETALHLVEKYLGKIINTSYLY
ETVPEYIDVNYINELMQNLEESKYEENKELIDKCEEYETFLKNGKVDNSI
LKEVNVENYLLECNNIIVKNDEIMKNSYFYNLTVVVKTFVNDPLSMLVVI
KYIEELMKRIIDIDILFFNDFTIFMKNIKLEKNMIYKILSKYIHLDPQEI
INNMVDNIEFLSIPHVYTTHRYSILLCLNDMIPEYKHNVLNNTIRCLYNK
YVSRMKEQYNINIKENNKRIYVLKDRISYLKEKTNIVGILNVNYDSFSDG
GIFVEPKRAVQRMFEMINEGASVIDIGGESSAPFVIPNPKISERDLVVPV
LQLFQKEWNDIKNKIVKCDAKPIISIDTINYNVFKECVDNDLVDILNDIS
ACTNNPEIIKLLKKKNKFYSVVLMHKRGNPHTMDKLTNYDNLVYDIKNYL
EQRLNFLVLNGIPRYRILFDIGLGFAKKHDQSIKLLQNIHVYDEYPLFIG
YSRKRFIAHCMNDQWMFQMNYMRKDKDQLLYQKNICGGLAIASYSYYKKV
DLIRVHDVLETKSVLDVLTKIDQVKDPNSSSVDKLAAALE
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 chain6jwq Chain B Residue 801 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB6jwq The structure of Plasmodium falciparum hydroxymethyldihydropterin pyrophosphokinase-dihydropteroate synthase reveals the basis of sulfa resistance.
Resolution2.5 Å
Binding residue
(original residue number in PDB)		D208 D210 I211 N312 E314 F315 L316 S317 H320
Binding residue
(residue number reindexed from 1)		D162 D164 I165 N207 E209 F210 L211 S212 H215
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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:6jwq, PDBe:6jwq, PDBj:6jwq
PDBsum6jwq
PubMed31883412
UniProtQ25704

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