Structure of PDB 3dga Chain B

Receptor sequence
>3dgaB (length=224) Species: 5833 (Plasmodium falciparum) [Search protein sequence]
MEQVCDVFDIYAICACCKVESKNEGKKNEVFNNYTFRGLGNKGVLPWKCN
SLDMKYFCAVTTYVNESKYEKLKYKRCKYLNKETVDNSKKLQNVVVMGRT
SWESIPKKFKPLSNRINVILSRTLKKEDFDEDVYIINKVEDLIVLLGKLN
YYKCFIIGGSVVYQEFLEKKLIKKIYFTRINSTYECDVFFPEINENEYQI
ISVSDVYTSNNTTLDFIIYKKTNN
3D structure
PDB3dga Exploiting structural analysis, in silico screening, and serendipity to identify novel inhibitors of drug-resistant falciparum malaria.
ChainB
Resolution2.7 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) L45 D53
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 RJ1 B D54 M55 F58 I164 D53 M54 F57 I157
BS02 NDP B A16 L40 G44 V45 L46 G105 R106 T107 S108 L127 S128 R129 T130 N144 I164 G166 S167 V168 V169 E172 A15 L39 G43 V44 L45 G98 R99 T100 S101 L120 S121 R122 T123 N137 I157 G159 S160 V161 V162 E165
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:3dga, PDBe:3dga, PDBj:3dga
PDBsum3dga
PubMed19146480
UniProtP13922|DRTS_PLAFK Bifunctional dihydrofolate reductase-thymidylate synthase

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