Structure of PDB 2o2s Chain A

Receptor sequence
>2o2sA (length=303) Species: 383379 (Toxoplasma gondii RH) [Search protein sequence]
PIDLRGQTAFVAGVADSHGYGWAIAKHLASAGARVALGTWPPVLGLFQKS
LQSGRLDEDRKLPDGSLIEFAGVYPLDAAFDKPEDVPQDIKDNKRYAGVD
GYTIKEVAVKVKQDLGNIDILVHSLANGPEVTKPLLETSRKGYLAASSNS
AYSFVSLLQHFGPIMNEGGSAVTLSYLAAERVVPGYGGGMSSAKAALESD
TRTLAWEAGQKYGVRVNAISAGPLKSRAASAIGKSGEKSFIDYAIDYSYN
NAPLRRDLHSDDVGGAALFLLSPLARAVSGVTLYVDNGLHAMGQAVDSRS
MPP
3D structure
PDB2o2s Studies of Toxoplasma gondii and Plasmodium falciparum enoyl acyl carrier protein reductase and implications for the development of antiparasitic agents
ChainA
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) Y186 K194
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 A18 G22 Y23 W43 D80 A81 S127 L128 A129 L177 S178 K197 P226 L227 S229 A231 A15 G19 Y20 W40 D77 A78 S124 L125 A126 L174 S175 K194 P223 L224 S226 A228
BS02 TCL A A129 N130 Y179 Y189 A231 A126 N127 Y176 Y186 A228 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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