Structure of PDB 1c14 Chain A

Receptor sequence
>1c14A (length=256) Species: 562 (Escherichia coli) [Search protein sequence]
GFLSGKRILVTGVASKLSIAYGIAQAMHREGAELAFTYQNDKLKGRVEEF
AAQLGSDIVLQCDVAEDASIDTMFAELGKVWPKFDGFVHSIGFAPGDQLD
GDYVNAVTREGFKIAHDISSYSFVAMAKACRSMLNPGSALLTLSYLGAER
AIPNYNVMGLAKASLEANVRYMANAMGPEGVRVNAISAGPIRTLAASGIK
DFRKMLAHCEAVTPIRRTVTIEDVGNSAAFLCSDLSAGISGEVVHVDGGF
SIAAMN
3D structure
PDB1c14 Molecular basis for triclosan activity involves a flipping loop in the active site.
ChainA
Resolution2.0 Å
3D
structure
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Enzymatic activity
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 A G13 A15 S19 I20 Q40 D64 V65 S91 I92 I119 L144 S145 K163 A189 P191 I192 T194 A196 G12 A14 S18 I19 Q39 D63 V64 S90 I91 I118 L143 S144 K162 A188 P190 I191 T193 A195
BS02 TCL A G93 A95 Y146 Y156 A196 A197 I200 F203 G92 A94 Y145 Y155 A195 A196 I199 F202 MOAD: ic50=120nM
BindingDB: IC50=430nM
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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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:1c14, PDBe:1c14, PDBj:1c14
PDBsum1c14
PubMed10595560
UniProtP0AEK4|FABI_ECOLI Enoyl-[acyl-carrier-protein] reductase [NADH] FabI (Gene Name=fabI)

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