Structure of PDB 2o2y Chain D

Receptor sequence
>2o2yD (length=288) Species: 36329 (Plasmodium falciparum 3D7) [Search protein sequence]
DICFIAGIGDTNGYGWGIAKELSKRNVKIIFGIWPPVYNIFMKNYKNGKF
DNDMIIDKDKKMNILDMLPFDASFDTANDIDEETKNNKRYNMLQNYTIED
VANLIHQKYGKINMLVHSLANAKEVQKDLLNTSRKGYLDALSKSSYSLIS
LCKYFVNIMKPQSSIISLTYHASQKVVPGYGGGMSSAKAALESDTRVLAY
HLGRNYNIRINTISAGPLKSRAATAIYTFIDYAIEYSEKYAPLRQKLLST
DIGSVASFLLSRESRAITGQTIYVDNGLNIMFLPDDIY
3D structure
PDB2o2y Studies of Toxoplasma gondii and Plasmodium falciparum enoyl acyl carrier protein reductase and implications for the development of antiparasitic agents
ChainD
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) Y180 K188
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 D G23 G27 Y28 W48 F84 D85 A86 S132 L133 A134 N135 L182 T183 Y184 K202 A229 G230 P231 L232 S234 R235 A236 G9 G13 Y14 W34 F70 D71 A72 S118 L119 A120 N121 L168 T169 Y170 K188 A215 G216 P217 L218 S220 R221 A222
BS02 TCL D A134 N135 A136 Y184 Y194 A236 A237 A120 N121 A122 Y170 Y180 A222 A223 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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