Structure of PDB 1j3k Chain A

Receptor sequence
>1j3kA (length=221) Species: 5833 (Plasmodium falciparum) [Search protein sequence]
MMEQVCDVFDIYAICACCKVESKNEGKKNEVFNNYTFRGLGNKGVLPWKC
ISLDMKYFRAVTTYVNESKYEKLKYKRCKYLNKETKKLQNVVVMGRTNWE
SIPKKFKPLSNRINVILSRTLKKEDFDEDVYIINKVEDLIVLLGKLNYYK
CFILGGSVVYQEFLEKKLIKKIYFTRINSTYECDVFFPEINENEYQIISV
SDVYTSNNTTLDFIIYKKTNN
3D structure
PDB1j3k Insights into antifolate resistance from malarial DHFR-TS structures.
ChainA
Resolution2.1 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
Catalytic site (residue number reindexed from 1) L46 D54
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 WRA A I14 C15 D54 M55 F58 N108 P113 I14 C15 D54 M55 F58 N98 P103 MOAD: Ki=0.037nM
BindingDB: IC50=0.570000nM,Ki=0.5nM
BS02 NDP A C15 A16 L40 G44 V45 L46 G105 R106 T107 N108 L127 S128 R129 T130 N144 L164 G165 G166 S167 V168 V169 E172 C15 A16 L40 G44 V45 L46 G95 R96 T97 N98 L117 S118 R119 T120 N134 L154 G155 G156 S157 V158 V159 E162
Gene Ontology
Molecular Function
GO:0004146 dihydrofolate reductase activity
GO:0050661 NADP binding
Biological Process
GO:0046654 tetrahydrofolate biosynthetic process

View graph for
Molecular Function
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Biological Process
External links
PDB RCSB:1j3k, PDBe:1j3k, PDBj:1j3k
PDBsum1j3k
PubMed12704428
UniProtP13922|DRTS_PLAFK Bifunctional dihydrofolate reductase-thymidylate synthase

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