Structure of PDB 5ifl Chain L

Receptor sequence

>5iflL (length=255) Species: 28450 (Burkholderia pseudomallei) [Search protein sequence]

GFLDGKRILLTGLLSNRSIAYGIAKACKREGAELAFTYVGDRFKDRITEF
AAEFGSELVFPCDVADDAQIDALFASLKTHWDSLDGLVHSIGFAPREAIA
GDFLDGLTRENFRIAHDISAYSFPALAKAALPMLSDDASLLTLSYLGAER
AIPNYNTMGLAKAALEASVRYLAVSLGAKGVRVNAISAGPIKTLAASGIK
SFGKILDFVESNSPLKRNVTIEQVGNAGAFLLSDLASGVTAEVMHVDSGF
NAVVG

3D structure

PDB

5ifl Rationalizing the Binding Kinetics for the Inhibition of the Burkholderia pseudomallei FabI1 Enoyl-ACP Reductase.

Chain

Resolution

2.6 Å

3D
structure

Catalytic site residues are labeled in the structure
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Enzymatic activity

Catalytic site (original residue number in PDB)	Y156 K163
Catalytic site (residue number reindexed from 1)	Y155 K162
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	TCL	L	G93 F94 A95 I100 Y146 Y156 A196 A197 I200 F203	G92 F93 A94 I99 Y145 Y155 A195 A196 I199 F202
BS02	NAD	L	G13 L15 S19 I20 V40 D64 V65 S91 I92 L144 S145 Y146 K163 A189 P191 I192 T194 A196	G12 L14 S18 I19 V39 D63 V64 S90 I91 L143 S144 Y145 K162 A188 P190 I191 T193 A195

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:5ifl, PDBe:5ifl, PDBj:5ifl
PDBsum	5ifl
PubMed	28225601
UniProt	A0A0H3HP34

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