Structure of PDB 5ifl Chain E Binding Site BS01
Receptor Information
>5ifl Chain E (length=255) Species:
28450
(Burkholderia pseudomallei) [
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GFLDGKRILLTGLLSNRSIAYGIAKACKREGAELAFTYVGDRFKDRITEF
AAEFGSELVFPCDVADDAQIDALFASLKTHWDSLDGLVHSIGFAPREAIA
GDFLDGLTRENFRIAHDISAYSFPALAKAALPMLSDDASLLTLSYLGAER
AIPNYNTMGLAKAALEASVRYLAVSLGAKGVRVNAISAGPIKTLAASGIK
SFGKILDFVESNSPLKRNVTIEQVGNAGAFLLSDLASGVTAEVMHVDSGF
NAVVG
Ligand information
Ligand ID
TCL
InChI
InChI=1S/C12H7Cl3O2/c13-7-1-3-11(9(15)5-7)17-12-4-2-8(14)6-10(12)16/h1-6,16H
InChIKey
XEFQLINVKFYRCS-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
Clc2cc(Cl)ccc2Oc1ccc(Cl)cc1O
OpenEye OEToolkits 1.5.0
c1cc(c(cc1Cl)O)Oc2ccc(cc2Cl)Cl
CACTVS 3.341
Oc1cc(Cl)ccc1Oc2ccc(Cl)cc2Cl
Formula
C12 H7 Cl3 O2
Name
TRICLOSAN
ChEMBL
CHEMBL849
DrugBank
DB08604
ZINC
ZINC000000002216
PDB chain
5ifl Chain E Residue 301 [
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Receptor-Ligand Complex Structure
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PDB
5ifl
Rationalizing the Binding Kinetics for the Inhibition of the Burkholderia pseudomallei FabI1 Enoyl-ACP Reductase.
Resolution
2.6 Å
Binding residue
(original residue number in PDB)
G93 A95 Y146 Y156 A196 I200 F203
Binding residue
(residue number reindexed from 1)
G92 A94 Y145 Y155 A195 I199 F202
Annotation score
1
Enzymatic activity
Catalytic site (original residue number in PDB)
Y156 K163
Catalytic site (residue number reindexed from 1)
Y155 K162
Enzyme Commision number
1.3.1.9
: enoyl-[acyl-carrier-protein] reductase (NADH).
Gene Ontology
Molecular Function
GO:0000166
nucleotide binding
GO:0004318
enoyl-[acyl-carrier-protein] reductase (NADH) activity
GO:0016491
oxidoreductase activity
Biological Process
GO:0006633
fatty acid biosynthetic process
View graph for
Molecular Function
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Biological Process
External links
PDB
RCSB:5ifl
,
PDBe:5ifl
,
PDBj:5ifl
PDBsum
5ifl
PubMed
28225601
UniProt
A0A0H3HP34
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