Structure of PDB 1nnu Chain A

Receptor sequence
>1nnuA (length=229) Species: 5833 (Plasmodium falciparum) [Search protein sequence]
EDICFIAGIGDTNGYGWGIAKELSKRNVKIIFGIWPPVYNIFMKNYKNGK
FDNDMIIDKDKKMNILDMLPFDASFDTANDIDEETKNNKRYNMLQNYTIE
DVANLIHQKYGKINMLVHSLANAKEVQKDLLNTSRKGYLDALSKSSYSLI
SLCKYFVNIMKPQSSIISLTYHASQKVVPGYGGGMSSAKAALESDTRVLA
YHLGRNYNIRINTISAGPLKSRAATAINK
3D structure
PDB1nnu Structural Elucidation of the Specificity of the Antibacterial Agent Triclosan for Malarial Enoyl Acyl Carrier Protein Reductase
ChainA
Resolution2.5 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) 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 NAD A G106 G110 Y111 W131 D168 A169 S215 L216 A217 N218 L265 T266 K285 A312 G313 P314 L315 S317 A319 G10 G14 Y15 W35 D72 A73 S119 L120 A121 N122 L169 T170 K189 A216 G217 P218 L219 S221 A223
BS02 TCT A A217 A219 V222 Y267 Y277 A319 I323 A121 A123 V126 Y171 Y181 A223 I227 MOAD: Ki=0.15uM
PDBbind-CN: -logKd/Ki=6.82,Ki=0.15uM
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:1nnu, PDBe:1nnu, PDBj:1nnu
PDBsum1nnu
PubMed11792710
UniProtQ9BH77

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