Structure of PDB 2o2y Chain C

Receptor sequence
>2o2yC (length=293) Species: 36329 (Plasmodium falciparum 3D7) [Search protein sequence]
NEDICFIAGIGDTNGYGWGIAKELSKRNVKIIFGIWPPVYNIFMKNYKNG
KFDNDMIIDKDKKMNILDMLPFDASFDTANDIDEETKNNKRYNMLQNYTI
EDVANLIHQKYGKINMLVHSLANAKEVQKDLLNTSRKGYLDALSKSSYSL
ISLCKYFVNIMKPQSSIISLTYHASQKVVPGYGGGMSSAKAALESDTRVL
AYHLGRNYNIRINTISAGPLKSRAATAINYTFIDYAIEYSEKYAPLRQKL
LSTDIGSVASFLLSRESRAITGQTIYVDNGLNIMFLPDDIYRN
3D structure
PDB2o2y Studies of Toxoplasma gondii and Plasmodium falciparum enoyl acyl carrier protein reductase and implications for the development of antiparasitic agents
ChainC
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y194 K202
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 C G23 G27 Y28 W48 D85 A86 S132 L133 N135 L182 T183 Y184 K202 A229 G230 P231 L232 S234 A236 G11 G15 Y16 W36 D73 A74 S120 L121 N123 L170 T171 Y172 K190 A217 G218 P219 L220 S222 A224
BS02 TCL C A134 N135 A136 Y184 Y194 M198 A236 A237 A122 N123 A124 Y172 Y182 M186 A224 A225 MOAD: Ki=0.4nM
BindingDB: IC50=49nM
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:2o2y, PDBe:2o2y, PDBj:2o2y
PDBsum2o2y
PubMed17327670
UniProtQ9BH77

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