Structure of PDB 2o2s Chain A Binding Site BS02

Receptor Information
>2o2s Chain A (length=303) Species: 383379 (Toxoplasma gondii RH) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
PIDLRGQTAFVAGVADSHGYGWAIAKHLASAGARVALGTWPPVLGLFQKS
LQSGRLDEDRKLPDGSLIEFAGVYPLDAAFDKPEDVPQDIKDNKRYAGVD
GYTIKEVAVKVKQDLGNIDILVHSLANGPEVTKPLLETSRKGYLAASSNS
AYSFVSLLQHFGPIMNEGGSAVTLSYLAAERVVPGYGGGMSSAKAALESD
TRTLAWEAGQKYGVRVNAISAGPLKSRAASAIGKSGEKSFIDYAIDYSYN
NAPLRRDLHSDDVGGAALFLLSPLARAVSGVTLYVDNGLHAMGQAVDSRS
MPP
Ligand information
Ligand IDTCL
InChIInChI=1S/C12H7Cl3O2/c13-7-1-3-11(9(15)5-7)17-12-4-2-8(14)6-10(12)16/h1-6,16H
InChIKeyXEFQLINVKFYRCS-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04Clc2cc(Cl)ccc2Oc1ccc(Cl)cc1O
OpenEye OEToolkits 1.5.0c1cc(c(cc1Cl)O)Oc2ccc(cc2Cl)Cl
CACTVS 3.341Oc1cc(Cl)ccc1Oc2ccc(Cl)cc2Cl
FormulaC12 H7 Cl3 O2
NameTRICLOSAN
ChEMBLCHEMBL849
DrugBankDB08604
ZINCZINC000000002216
PDB chain2o2s Chain A Residue 705 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB2o2s Studies of Toxoplasma gondii and Plasmodium falciparum enoyl acyl carrier protein reductase and implications for the development of antiparasitic agents
Resolution2.6 Å
Binding residue
(original residue number in PDB)		A129 N130 Y179 Y189 A231
Binding residue
(residue number reindexed from 1)		A126 N127 Y176 Y186 A228
Annotation score1
Binding affinityBindingDB: IC50=15nM
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).
Gene Ontology
Molecular Function
GO:0004318 enoyl-[acyl-carrier-protein] reductase (NADH) activity
Biological Process
GO:0006633 fatty acid biosynthetic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:2o2s, PDBe:2o2s, PDBj:2o2s
PDBsum2o2s
PubMed17327670
UniProtQ6UCJ9

[Back to BioLiP]