Structure of PDB 3lt2 Chain B

Receptor sequence

>3lt2B (length=287) Species: 5833 (Plasmodium falciparum) [Search protein sequence]

NEDICFIAGIGDTNGYGWGIAKELSKRNVKIIFGIWPPVYNIFMKNYKNG
KFDNDMIIDKDKKMNILDMLPFDASFDTANDIDEETKNNKRYNMLQNYTI
EDVANLIHQKYGKINMLVHSLANAKEVQKDLLNTSRKGYLDALSKSSYSL
ISLCKYFVNIMKPQSSIISLTYHASQKVVPGYGGGMSSAKAALESDTRVL
AYHLGRNYNIRINTISAGPLKSRAATAINTFIDYAIEYSEKYAPLRQKLL
STDIGSVASFLLSRESRAITGQTIYVDNGLNIMFLPD

3D structure

PDB

3lt2 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

Chain

Resolution

2.5 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	B	G106 G110 Y111 W131 F167 D168 A169 S215 L216 A217 N218 L265 T266 Y267 K285 A312 G313 P314 L315 S317 A319	G11 G15 Y16 W36 F72 D73 A74 S120 L121 A122 N123 L170 T171 Y172 K190 A217 G218 P219 L220 S222 A224
BS02	FT3	B	A217 N218 A219 V222 Y267 Y277 P314 A319 A320	A122 N123 A124 V127 Y172 Y182 P219 A224 A225	MOAD: Ki=0.38uM

Gene Ontology

	Molecular Function
GO:0004318	enoyl-[acyl-carrier-protein] reductase (NADH) activity

	Biological Process
GO:0006633	fatty acid biosynthetic process

View graph for
Molecular Function

View graph for
Biological Process

External links

PDB	RCSB:3lt2, PDBe:3lt2, PDBj:3lt2
PDBsum	3lt2
PubMed	20503440
UniProt	Q9BJJ9

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