Structure of PDB 4ige Chain B

Receptor sequence
>4igeB (length=287) Species: 36329 (Plasmodium falciparum 3D7) [Search protein sequence]
EDICFIAGIGDTNGYGWGIAKELSKRNVKIIFGIWPPVYNIFMKNYKNGK
FDNDMIIDKDKKMNILDMLPFDASFDTANDIDEETKNNKRYNMLQNYTIE
DVANLIHQKYGKINMLVHSLANAKEVQKDLLNTSRKGYLDALSKSSYSLI
SLCKYFVNIMKPQSSIISLTYHASQKVVPGYGGGMSSAKAALESDTRVLA
YHLGRNYNIRINTISAGPLKSRAATAINKTFIDYAIEYSEKYAPLRQKLL
STDIGSVASFLLSRESRAITGQTIYVDNGLNIMFLPD
3D structure
PDB4ige Design, Synthesis, and Biological and Crystallographic Evaluation of Novel Inhibitors of Plasmodium falciparum Enoyl-ACP-reductase (PfFabI)
ChainB
Resolution2.15 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) Y181 K189
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 CHJ B A217 N218 A219 Y267 Y277 A319 A320 A121 N122 A123 Y171 Y181 A223 A224 MOAD: ic50=0.25uM
BS02 NAD B G106 G110 Y111 W131 F167 D168 A169 S215 L216 A217 N218 L265 T266 Y267 K285 A312 P314 L315 S317 A319 G10 G14 Y15 W35 F71 D72 A73 S119 L120 A121 N122 L169 T170 Y171 K189 A216 P218 L219 S221 A223
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:4ige, PDBe:4ige, PDBj:4ige
PDBsum4ige
PubMed24063369
UniProtC6KSZ2

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