Structure of PDB 4j4t Chain B

Receptor sequence

>4j4tB (length=259) Species: 177416 (Francisella tularensis subsp. tularensis SCHU S4)

GFLAGKKILITGLLSNKSIAYGIAKAMHREGAELAFTYVGQFKDRVEKLC
AEFNPAAVLPCDVISDQEIKDLFVELGKVWDGLDAIVHSIAFAPRDQLEG
NFIDCVTREGFSIAHDISAYSFAALAKEGRSMMKNRNASMVALTYIGAEK
AMPSYNTMGVAKASLEATVRYTALALGEDGIKVNAVSAGPIKTLAASGIS
NFKKMLDYNAMVSPLKKNVDIMEVGNTVAFLCSDMATGITGEVVHVDAGY
HCVSMGNVL

3D structure

• PDB: 4j4t Structural and biological evaluation of a novel series of benzimidazole inhibitors of Francisella tularensis enoyl-ACP reductase (FabI).
• Chain: B
• Resolution: 2.34 Å

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	NAD	B	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
BS02	1JU	B	A92 F93 L99 Y146 Y156 M159 A196 F203 M206	A91 F92 L98 Y145 Y155 M158 A195 F202 M205

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

External links

• PDB: RCSB:4j4t, PDBe:4j4t, PDBj:4j4t
• PDBsum: 4j4t
• PubMed: 25677657
• UniProt: Q5NGQ3