Structure of PDB 1j3j Chain C Binding Site BS01

Receptor Information
>1j3j Chain C (length=326) Species: 5833 (Plasmodium falciparum) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
DDEEEDDFVYFNFNKEKEEKNKNSIHPNDFQIYNSLKYKYHPEYQYLNII
YDIMMNGNKQSDRTGVGVLSKFGYIMKFDLSQYFPLLTTKKLFLRGIIEE
LLWFIRGETNGNTLLNKNVRIWEANGTREFLDNRKLFHREVNDLGPIYGF
QWRHFGAEYTNMYDNYENKGVDQLKNIINLIKNDPTSRRILLCAWNVKDL
DQMALPPCHILCQFYVFDGKLSCIMYQRSCDLGLGVPFNIASYSIFTHMI
AQVCNLQPAQFIHVLGNAHVYNNHIDSLKIQLNRIPYPFPTLKLNPDIKN
IEDFTISDFTIQNYVHHEKISMDMAA
Ligand information
Ligand IDUMP
InChIInChI=1S/C9H13N2O8P/c12-5-3-8(11-2-1-7(13)10-9(11)14)19-6(5)4-18-20(15,16)17/h1-2,5-6,8,12H,3-4H2,(H,10,13,14)(H2,15,16,17)/t5-,6+,8+/m0/s1
InChIKeyJSRLJPSBLDHEIO-SHYZEUOFSA-N
SMILES
SoftwareSMILES
ACDLabs 12.01O=P(O)(O)OCC2OC(N1C(=O)NC(=O)C=C1)CC2O
CACTVS 3.370O[CH]1C[CH](O[CH]1CO[P](O)(O)=O)N2C=CC(=O)NC2=O
OpenEye OEToolkits 1.7.6C1[C@@H]([C@H](O[C@H]1N2C=CC(=O)NC2=O)COP(=O)(O)O)O
CACTVS 3.370O[C@H]1C[C@@H](O[C@@H]1CO[P](O)(O)=O)N2C=CC(=O)NC2=O
OpenEye OEToolkits 1.7.6C1C(C(OC1N2C=CC(=O)NC2=O)COP(=O)(O)O)O
FormulaC9 H13 N2 O8 P
Name2'-DEOXYURIDINE 5'-MONOPHOSPHATE;
DUMP
ChEMBLCHEMBL211312
DrugBankDB03800
ZINCZINC000004228260
PDB chain1j3j Chain C Residue 611 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1j3j Insights into antifolate resistance from malarial DHFR-TS structures.
Resolution2.3 Å
Binding residue
(original residue number in PDB)		C490 H491 R510 S511 D513 N521 H551
Binding residue
(residue number reindexed from 1)		C208 H209 R228 S229 D231 N239 H269
Annotation score3
Enzymatic activity
Catalytic site (original residue number in PDB) E382 W404 Y430 C490 R510 D513
Catalytic site (residue number reindexed from 1) E100 W122 Y148 C208 R228 D231
Enzyme Commision number 1.5.1.3: dihydrofolate reductase.
2.1.1.45: thymidylate synthase.
Gene Ontology
Molecular Function
GO:0004799 thymidylate synthase activity
GO:0016741 transferase activity, transferring one-carbon groups
Biological Process
GO:0006231 dTMP biosynthetic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1j3j, PDBe:1j3j, PDBj:1j3j
PDBsum1j3j
PubMed12704428
UniProtP13922|DRTS_PLAFK Bifunctional dihydrofolate reductase-thymidylate synthase

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