Structure of PDB 3jsu Chain B

Receptor sequence
>3jsuB (length=542) Species: 5833 (Plasmodium falciparum) [Search protein sequence]
MEQVCDVFDIYAICACCKVESKNEGKKNEVFNNYTFRGLGNKGVLPWKCI
SLDMKYFRAVTTYVNESKYEKLKYKRCKYLPNSKKLQNVVVMGRTNWESI
PKKFKPLSNRINVILSRTLKKEDFDEDVYIINKVEDLIVLLGKLNYYKCF
ILGGSVVYQEFLEKKLIKKIYFTRINSTYECDVFFPEINENEYQIISVSD
VYTSNNTTLDFIIYKKTNNDDEEEDDFVYFNFNKEKEEKNKNSIHPNDFQ
IYNSLKYKYHPEYQYLNIIYDIMMNGNKQSDRTGVGVLSKFGYIMKFDLS
QYFPLLTTKKLFLRGIIEELLWFIRGETNGNTLLNKNVRIWEANGTREFL
DNRKLFHREVNDLGPIYGFQWRHFGAEYTNMYDNYENKGVDQLKNIINLI
KNDPTSRRILLCAWNVKDLDQMALPPCHILCQFYVFDGKLSCIMYQRSCD
LGLGVPFNIASYSIFTHMIAQVCNLQPAQFIHVLGNAHVYNNHIDSLKIQ
LNRIPYPFPTLKLNPDIKNIEDFTISDFTIQNYVHHEKISMD
3D structure
PDB3jsu Preclinical evaluation of the antifolate QN254, 5-chloro- N'6'-(2,5-dimethoxy-benzyl)-quinazoline-2,4,6-triamine, as an antimalarial drug candidate
ChainB
Resolution2.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) L46 D54 E382 W404 Y430 C490 R510 D513
Catalytic site (residue number reindexed from 1) L45 D53 E319 W341 Y367 C427 R447 D450
Enzyme Commision number 1.5.1.3: dihydrofolate reductase.
2.1.1.45: thymidylate synthase.
Interaction with ligand
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0004146 dihydrofolate reductase activity
GO:0004799 thymidylate synthase activity
GO:0008168 methyltransferase activity
GO:0016491 oxidoreductase activity
GO:0016741 transferase activity, transferring one-carbon groups
Biological Process
GO:0006231 dTMP biosynthetic process
GO:0006730 one-carbon metabolic process
GO:0009165 nucleotide biosynthetic process
GO:0032259 methylation
GO:0046654 tetrahydrofolate biosynthetic process
Cellular Component
GO:0005739 mitochondrion
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3jsu, PDBe:3jsu, PDBj:3jsu
PDBsum3jsu
PubMed20350951
UniProtD9N170

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