Structure of PDB 3lt1 Chain B

Receptor sequence

>3lt1B (length=289) Species: 5833 (Plasmodium falciparum)

NEDICFIAGIGDTNGYGWGIAKELSKRNVKIIFGIWPPVYNIFMKNYKNG
KFDNDMIIDKDKKMNILDMLPFDASFDTANDIDEETKNNKRYNMLQNYTI
EDVANLIHQKYGKINMLVHSLANAKEVQKDLLNTSRKGYLDALSKSSYSL
ISLCKYFVNIMKPQSSIISLTYHASQKVVPGYGGGMSSAKAALESDTRVL
AYHLGRNYNIRINTISAGPLKSRAATAINKLTFIDYAIEYSEKYAPLRQK
LLSTDIGSVASFLLSRESRAITGQTIYVDNGLNIMFLPD

3D structure

• PDB: 3lt1 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: B
• Resolution: 2.2 Å

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 N218 L265 T266 Y267 K285 A312 P314 L315 S317 A319	G11 G15 Y16 W36 F72 D73 A74 S120 L121 N123 L170 T171 Y172 K190 A217 P219 L220 S222 A224
BS02	FT2	B	A217 N218 A219 V222 Y267 Y277 P314 A319 A320 I323	A122 N123 A124 V127 Y172 Y182 P219 A224 A225 I228	MOAD: Ki=0.32uM

Gene Ontology

Molecular Function

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

Biological Process

• GO:0006633 fatty acid biosynthetic process

External links

• PDB: RCSB:3lt1, PDBe:3lt1, PDBj:3lt1
• PDBsum: 3lt1
• PubMed: 20503440
• UniProt: Q9BJJ9