Structure of PDB 1j3j Chain A

Receptor sequence
>1j3jA (length=221) Species: 5833 (Plasmodium falciparum) [Search protein sequence]
MMEQVCDVFDIYAICACCKVESKNEGKKNEVFNNYTFRGLGNKGVLPWKC
NSLDMKYFRAVTTYVNESKYEKLKYKRCKYLNKETKKLQNVVVMGRTNWE
SIPKKFKPLSNRINVILSRTLKKEDFDEDVYIINKVEDLIVLLGKLNYYK
CFIIGGSVVYQEFLEKKLIKKIYFTRINSTYECDVFFPEINENEYQIISV
SDVYTSNNTTLDFIIYKKTNN
3D structure
PDB1j3j Insights into antifolate resistance from malarial DHFR-TS structures.
ChainA
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 CP6 A I14 C15 A16 D54 F58 N108 I112 I164 I14 C15 A16 D54 F58 N98 I102 I154 MOAD: Ki=9.8nM
BindingDB: Ki=0.6nM,IC50=30900nM
BS02 NDP A C15 A16 L40 G44 V45 L46 W48 G105 R106 T107 N108 L127 S128 R129 T130 N144 I164 G165 G166 S167 V168 V169 Y170 E172 V195 C15 A16 L40 G44 V45 L46 W48 G95 R96 T97 N98 L117 S118 R119 T120 N134 I154 G155 G156 S157 V158 V159 Y160 E162 V185
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
View graph for
Biological Process
External links
PDB RCSB:1j3j, PDBe:1j3j, PDBj:1j3j
PDBsum1j3j
PubMed12704428
UniProtP13922|DRTS_PLAFK Bifunctional dihydrofolate reductase-thymidylate synthase

[Back to BioLiP]