Structure of PDB 1j3i Chain D

Receptor sequence
>1j3iD (length=328) Species: 5833 (Plasmodium falciparum) [Search protein sequence]
DDDDEEEDDFVYFNFNKEKEEKNKNSIHPNDFQIYNSLKYKYHPEYQYLN
IIYDIMMNGNKQSDRTGVGVLSKFGYIMKFDLSQYFPLLTTKKLFLRGII
EELLWFIRGETNGNTLLNKNVRIWEANGTREFLDNRKLFHREVNDLGPIY
GFQWRHFGAEYTNMYDNYENKGVDQLKNIINLIKNDPTSRRILLCAWNVK
DLDQMALPPCHILCQFYVFDGKLSCIMYQRSCDLGLGVPFNIASYSIFTH
MIAQVCNLQPAQFIHVLGNAHVYNNHIDSLKIQLNRIPYPFPTLKLNPDI
KNIEDFTISDFTIQNYVHHEKISMDMAA
3D structure
PDB1j3i Insights into antifolate resistance from malarial DHFR-TS structures.
ChainD
Resolution2.33 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) E382 W404 Y430 C490 R510 D513
Catalytic site (residue number reindexed from 1) E102 W124 Y150 C210 R230 D233
Enzyme Commision number 1.5.1.3: dihydrofolate reductase.
2.1.1.45: thymidylate synthase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 UMP D R470 R471 R190 R191
BS02 UMP D R345 C490 H491 Q509 R510 S511 D513 G517 N521 H551 Y553 R65 C210 H211 Q229 R230 S231 D233 G237 N241 H271 Y273
Gene Ontology
Molecular Function
GO:0004799 thymidylate synthase activity
GO:0016741 transferase activity, transferring one-carbon groups
Biological Process
GO:0006231 dTMP biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:1j3i, PDBe:1j3i, PDBj:1j3i
PDBsum1j3i
PubMed12704428
UniProtP13922|DRTS_PLAFK Bifunctional dihydrofolate reductase-thymidylate synthase

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