Structure of PDB 5ifl Chain J

Receptor sequence
>5iflJ (length=255) Species: 28450 (Burkholderia pseudomallei) [Search protein sequence]
GFLDGKRILLTGLLSNRSIAYGIAKACKREGAELAFTYVGDRFKDRITEF
AAEFGSELVFPCDVADDAQIDALFASLKTHWDSLDGLVHSIGFAPREAIA
GDFLDGLTRENFRIAHDISAYSFPALAKAALPMLSDDASLLTLSYLGAER
AIPNYNTMGLAKAALEASVRYLAVSLGAKGVRVNAISAGPIKTLAASGIK
SFGKILDFVESNSPLKRNVTIEQVGNAGAFLLSDLASGVTAEVMHVDSGF
NAVVG
3D structure
PDB5ifl Rationalizing the Binding Kinetics for the Inhibition of the Burkholderia pseudomallei FabI1 Enoyl-ACP Reductase.
ChainJ
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) 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 J G93 A95 I100 Y146 Y156 A196 I200 F203 G92 A94 I99 Y145 Y155 A195 I199 F202
BS02 NAD J G13 L15 S19 I20 V40 D64 V65 S91 I92 I119 L144 S145 Y146 K163 A189 P191 I192 T194 A196 G12 L14 S18 I19 V39 D63 V64 S90 I91 I118 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

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Molecular Function
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Biological Process
External links
PDB RCSB:5ifl, PDBe:5ifl, PDBj:5ifl
PDBsum5ifl
PubMed28225601
UniProtA0A0H3HP34

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