Structure of PDB 3lt0 Chain A

Receptor sequence
>3lt0A (length=287) Species: 5833 (Plasmodium falciparum) [Search protein sequence]
NEDICFIAGIGDTNGYGWGIAKELSKRNVKIIFGIWPPVYNIFMKNYKNG
KFDNDMIIDKDKKMNILDMLPFDASFDTANDIDEETKNNKRYNMLQNYTI
EDVANLIHQKYGKINMLVHSLANAKEVQKDLLNTSRKGYLDALSKSSYSL
ISLCKYFVNIMKPQSSIISLTYHASQKVVPGYGGGMSSAKAALESDTRVL
AYHLGRNYNIRINTISAGPLKSRAATAINTFIDYAIEYSEKYAPLRQKLL
STDIGSVASFLLSRESRAITGQTIYVDNGLNIMFLPD
3D structure
PDB3lt0 X-ray crystallographic analysis of the complexes of enoyl acyl carrier protein reductase of Plasmodium falciparum with triclosan variants to elucidate the importance of different functional groups in enzyme inhibition
ChainA
Resolution1.96 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y277 K285
Catalytic site (residue number reindexed from 1) Y182 K190
Enzyme Commision number 1.3.1.9: enoyl-[acyl-carrier-protein] reductase (NADH).
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 NAD A G106 G110 Y111 W131 D168 A169 S215 L216 A217 N218 L265 T266 Y267 K285 A312 P314 L315 S317 A319 G11 G15 Y16 W36 D73 A74 S120 L121 A122 N123 L170 T171 Y172 K190 A217 P219 L220 S222 A224
BS02 FT1 A A217 N218 A219 Y267 Y277 A319 A320 I323 A122 N123 A124 Y172 Y182 A224 A225 I228 MOAD: Ki=0.18uM
Gene Ontology
Molecular Function
GO:0004318 enoyl-[acyl-carrier-protein] reductase (NADH) activity
Biological Process
GO:0006633 fatty acid biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:3lt0, PDBe:3lt0, PDBj:3lt0
PDBsum3lt0
PubMed20503440
UniProtQ9BJJ9

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