Structure of PDB 4j3f Chain A

Receptor sequence
>4j3fA (length=259) Species: 177416 (Francisella tularensis subsp. tularensis SCHU S4) [Search protein sequence]
GFLAGKKILITGLLSNKSIAYGIAKAMHREGAELAFTYVGQFKDRVEKLC
AEFNPAAVLPCDVISDQEIKDLFVELGKVWDGLDAIVHSIAFAPRDQLEG
NFIDCVTREGFSIAHDISAYSFAALAKEGRSMMKNRNASMVALTYIGAEK
AMPSYNTMGVAKASLEATVRYTALALGEDGIKVNAVSAGPIKTLAASGIS
NFKKMLDYNAMVSPLKKNVDIMEVGNTVAFLCSDMATGITGEVVHVDAGY
HCVSMGNVL
3D structure
PDB4j3f Structural and biological evaluation of a novel series of benzimidazole inhibitors of Francisella tularensis enoyl-ACP reductase (FabI).
ChainA
Resolution1.85 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) M28 A33 C51 N55 P56 A57 D117 T145 Y156 M159 K163 T194
Catalytic site (residue number reindexed from 1) M27 A32 C50 N54 P55 A56 D116 T144 Y155 M158 K162 T193
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 1JT A Y146 P154 Y156 A196 F203 M206 Y145 P153 Y155 A195 F202 M205
BS02 NAD A G13 L15 S19 I20 V40 D63 V64 S90 I91 A92 L144 T145 Y146 K163 A189 P191 I192 T194 A196 G12 L14 S18 I19 V39 D62 V63 S89 I90 A91 L143 T144 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:4j3f, PDBe:4j3f, PDBj:4j3f
PDBsum4j3f
PubMed25677657
UniProtQ5NGQ3

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