Structure of PDB 6leu Chain B

Receptor sequence
>6leuB (length=529) Species: 5833 (Plasmodium falciparum) [Search protein sequence]
QVCDVFDIYAICACCKVEEVFNNYTFRGLGNKGVLPWKCISLDMKYFRAV
TTYVNESKYEKLKYKRCKYLKLQNVVVMGRTNWESIPKKFKPLSNRINVI
LSRTLKKEDFDEDVYIINKVEDLIVLLGKLNYYKCFILGGSVVYQEFLEK
KLIKKIYFTRINSTYECDVFFPEINENEYQIISVSDVYTSNNTTLDFIIY
KKTNNDDEEEDDFVYFNFNKEKEEKNKNSIHPNDFQIYNSLKYKYHPEYQ
YLNIIYDIMMNGNKQSDRTGVGVLSKFGYIMKFDLSQYFPLLTTKKLFLR
GIIEELLWFIRGETNGNTLLNKNVRIWEANGTREFLDNRKLFHREVNDLG
PIYGFQWRHFGAEYTNMYDNYENKGVDQLKNIINLIKNDPTSRRILLCAW
NVKDLDQMALPPCHILCQFYVFDGKLSCIMYQRSCDLGLGVPFNIASYSI
FTHMIAQVCNLQPAQFIHVLGNAHVYNNHIDSLKIQLNRIPYPFPTLKLN
PDIKNIEDFTISDFTIQNYVHHEKISMDM
3D structure
PDB6leu Flexible diaminodihydrotriazine inhibitors of Plasmodium falciparum dihydrofolate reductase: Binding strengths, modes of binding and their antimalarial activities.
ChainB
Resolution2.59 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) L35 D43 E305 W327 Y353 C413 R433 D436
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:6leu, PDBe:6leu, PDBj:6leu
PDBsum6leu
PubMed32294614
UniProtD9N170

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