Structure of PDB 1dfh Chain A

Receptor sequence
>1dfhA (length=257) Species: 562 (Escherichia coli) [Search protein sequence]
GFLSGKRILVTGVASKLSIAYGIAQAMHREGAELAFTYQNDKLKGRVEEF
AAQLGSDIVLQCDVAEDASIDTMFAELGKVWPKFDGFVHSIGFAPGDQLD
GDYVNAVTREGFKIAHDISSYSFVAMAKACRSMLNPGSALLTLSYLGAER
AIPNYNVMGLAKASLEANVRYMANAMGPEGVRVNAISAGPIRTLAASGIK
DFRKMLAHCEAVTPIRRTVTIEDVGNSAAFLCSDLSAGISGEVVHVDGGF
SIAAMNE
3D structure
PDB1dfh A mechanism of drug action revealed by structural studies of enoyl reductase.
ChainA
Resolution2.2 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 I200
Catalytic site (residue number reindexed from 1) S144 Y155 M158 K162 I199
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 S145 K163 A189 P191 I192 G12 A14 S18 I19 Q39 D63 V64 S90 I91 S144 K162 A188 P190 I191
BS02 TDB A G93 Y146 Y156 I200 G92 Y145 Y155 I199
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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Cellular Component
External links
PDB RCSB:1dfh, PDBe:1dfh, PDBj:1dfh
PDBsum1dfh
PubMed8953047
UniProtP0AEK4|FABI_ECOLI Enoyl-[acyl-carrier-protein] reductase [NADH] FabI (Gene Name=fabI)

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