Structure of PDB 2o2s Chain B

Receptor sequence
>2o2sB (length=302) Species: 383379 (Toxoplasma gondii RH) [Search protein sequence]
FPIDLRGQTAFVAGVADSHGYGWAIAKHLASAGARVALGTWPPVLGLFQK
SLQSGRLDEDRKLPDGSLIEFAGVYPLDAAFDKPEDVPQDIKDNKRYAGV
DGYTIKEVAVKVKQDLGNIDILVHSLANGPEVTKPLLETSRKGYLAASSN
SAYSFVSLLQHFGPIMNEGGSAVTLSYLAAERVVPGYGGGMSSAKAALES
DTRTLAWEAGQKYGVRVNAISAGPLKSRAASAIGKEKSFIDYAIDYSYNN
APLRRDLHSDDVGGAALFLLSPLARAVSGVTLYVDNGLHAMGQAVDSRSM
PP
3D structure
PDB2o2s Studies of Toxoplasma gondii and Plasmodium falciparum enoyl acyl carrier protein reductase and implications for the development of antiparasitic agents
ChainB
Resolution2.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y189 K197
Catalytic site (residue number reindexed from 1) Y187 K195
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 G16 G22 Y23 W43 D80 A81 S127 L128 A129 L177 S178 K197 G225 P226 L227 S229 A231 G14 G20 Y21 W41 D78 A79 S125 L126 A127 L175 S176 K195 G223 P224 L225 S227 A229
BS02 TCL B A129 G131 Y179 Y189 M193 A231 A232 A127 G129 Y177 Y187 M191 A229 A230 BindingDB: IC50=15nM
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:2o2s, PDBe:2o2s, PDBj:2o2s
PDBsum2o2s
PubMed17327670
UniProtQ6UCJ9

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