Structure of PDB 6jwr Chain A Binding Site BS02

Receptor Information
>6jwr Chain A (length=549) Species: 5833 (Plasmodium falciparum) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
IQELILSEENKTNIAVLNLGTNDRRNAVLILETALHLVEKYLGKIINTSY
LYETVPEYIVLDDVNYINELMQNLEESKYEENKELIDKCEEYETFLKNGK
VDNSILKEVNVENYLLECNNIIVKNDEIMKNNTSYFYNLTVVVKTFVNDP
LSMLVVIKYIEELMKIIDIDILFFNDFTIFMKNIKLEKNMIYKILSKYIH
LEIINNMVDNIEFLSIPHVYTTHRYSILLCLNDMIPEYKHNVLNNTIRCL
YNKYVSRMKEQYNINIKENNKRIYVLKDRISYLKEKTNIVGILNVNIFVE
PKRAVQRMFEMINEGASVIDIGGESSAPFVIPNPKISERDLVVPVLQLFQ
KEWNDIAKPIISIDTINYNVFKECVDNDLVDILNDISACTNNPEIIKLLK
KKNKFYSVVLMHKRGNPHTMDKLTNYDNLVYDIKNYLEQRLNFLVLNGIP
RYRILFDIGLGFAKKHDQSIKLLQNIHVYDEYPLFIGYSRKRFIAHCMND
KDQLLYQKNICGGLAIASYSYYKKVDLIRVHDVLETKSVLDVLTKIDQV
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 chain6jwr Chain A Residue 802 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB6jwr The structure of Plasmodium falciparum hydroxymethyldihydropterin pyrophosphokinase-dihydropteroate synthase reveals the basis of sulfa resistance.
Resolution2.6 Å
Binding residue
(original residue number in PDB)		L181 I211 N312 F315 L316 S317 H320
Binding residue
(residue number reindexed from 1)		L154 I171 N210 F213 L214 S215 H218
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:6jwr, PDBe:6jwr, PDBj:6jwr
PDBsum6jwr
PubMed31883412
UniProtQ25704

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