Structure of PDB 5i7f Chain J Binding Site BS02

Receptor Information
>5i7f Chain J (length=257) Species: 28450 (Burkholderia pseudomallei) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
GFLDGKRILLTGLLSNRSIAYGIAKACKREGAELAFTYVGDRFKDRITEF
AAEFGSELVFPCDVADDAQIDALFASLKTHWDSLDGLVHSIGFAPREAIA
GDFLDGLTRENFRIAHDISAYSFPALAKAALPMLSDDASLLTLSYLGAER
AIPNYNTMGLAKAALEASVRYLAVSLGAKGVRVNAISAGPIKTLAASGIK
SFGKILDFVESNSPLKRNVTIEQVGNAGAFLLSDLASGVTAEVMHVDSGF
NAVVGGM
Ligand information
Ligand ID68O
InChIInChI=1S/C14H12F2O2/c1-2-9-7-12(17)14(8-11(9)16)18-13-6-4-3-5-10(13)15/h3-8,17H,2H2,1H3
InChIKeyMUHZCNPYLSMOCX-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.385CCc1cc(O)c(Oc2ccccc2F)cc1F
ACDLabs 12.01Fc1c(cccc1)Oc2cc(F)c(CC)cc2O
OpenEye OEToolkits 2.0.4CCc1cc(c(cc1F)Oc2ccccc2F)O
FormulaC14 H12 F2 O2
Name5-ethyl-4-fluoro-2-(2-fluorophenoxy)phenol
ChEMBLCHEMBL2178304
DrugBank
ZINCZINC000095574586
PDB chain5i7f Chain J Residue 302 [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]
PDB5i7f Rationalizing the Binding Kinetics for the Inhibition of the Burkholderia pseudomallei FabI1 Enoyl-ACP Reductase.
Resolution2.7 Å
Binding residue
(original residue number in PDB)		Y146 Y156 M159 A196 A197 I200 F203
Binding residue
(residue number reindexed from 1)		Y145 Y155 M158 A195 A196 I199 F202
Annotation score1
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
View graph for
Biological Process
External links
PDB RCSB:5i7f, PDBe:5i7f, PDBj:5i7f
PDBsum5i7f
PubMed28225601
UniProtA0A0H3HP34

[Back to BioLiP]