Structure of PDB 1lx6 Chain B

Receptor sequence
>1lx6B (length=243) Species: 562 (Escherichia coli) [Search protein sequence]
GFLSGKRILVTGVASKLSIAYGIAQAMHREGAELAFTYQNDKLKGRVEEF
AAQLGSDIVLQCDVAEDASIDTMFAELGKVWPKFDGFVHSIGFAPGDQLD
GDYVNAVTREGFKIAHDISSYSFVAMAKACRSMLNPGSALLTLSYLGAER
AIPNYNVMGLAKASLEANVRYMANAMGPEGVRVNAISAGPIMLAHCEAVT
PIRRTVTIEDVGNSAAFLCSDLSAGISGEVVHVDGGFSIAAMN
3D structure
PDB1lx6 Discovery of aminopyridine-based inhibitors of bacterial enoyl-ACP reductase (FabI).
ChainB
Resolution2.4 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S145 Y156 M159 K163
Catalytic site (residue number reindexed from 1) S144 Y155 M158 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 NAD B G13 S19 I20 Q40 C63 D64 V65 S91 I92 S145 Y146 K163 P191 I192 G12 S18 I19 Q39 C62 D63 V64 S90 I91 S144 Y145 K162 P190 I191
BS02 ZAM B G93 Y146 N155 Y156 M206 G92 Y145 N154 Y155 M192
Gene Ontology
Molecular Function
GO:0004318 enoyl-[acyl-carrier-protein] reductase (NADH) activity
GO:0005515 protein binding
GO:0016491 oxidoreductase activity
GO:0042802 identical protein binding
GO:0070404 NADH binding
Biological Process
GO:0006633 fatty acid biosynthetic process
GO:0008610 lipid biosynthetic process
GO:0009102 biotin biosynthetic process
GO:0030497 fatty acid elongation
GO:0046677 response to antibiotic
GO:0051289 protein homotetramerization
Cellular Component
GO:0005829 cytosol
GO:0016020 membrane
GO:0032991 protein-containing complex
GO:1902494 catalytic complex

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Biological Process
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Cellular Component
External links
PDB RCSB:1lx6, PDBe:1lx6, PDBj:1lx6
PDBsum1lx6
PubMed12109908
UniProtP0AEK4|FABI_ECOLI Enoyl-[acyl-carrier-protein] reductase [NADH] FabI (Gene Name=fabI)

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