Structure of PDB 1d7o Chain A

Receptor sequence
>1d7oA (length=297) Species: 3708 (Brassica napus) [Search protein sequence]
GLPIDLRGKRAFIAGIADDNGYGWAVAKSLAAAGAEILVGTWVPALNIFE
TSLRRGKFDQSRVLPDGSLMEIKKVYPLDAVFDNPEDVPEDVKANKRYAG
SSNWTVQEAAECVRQDFGSIDILVHSLANGPEVSKPLLETSRKGYLAAIS
ASSYSFVSLLSHFLPIMNPGGASISLTYIASERIIPGYGGGMSSAKAALE
SDTRVLAFEAGRKQNIRVNTISAGPLGSRAAKAIGFIDTMIEYSYNNAPI
QKTLTADEVGNAAAFLVSPLASAITGATIYVDNGLNSMGVALDSPVF
3D structure
PDB1d7o Crystallographic analysis of triclosan bound to enoyl reductase.
ChainA
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y198 K206
Catalytic site (residue number reindexed from 1) Y188 K196
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 G25 G31 Y32 W52 D89 S136 L137 A138 N139 L186 T187 Y188 K206 P235 G15 G21 Y22 W42 D79 S126 L127 A128 N129 L176 T177 Y178 K196 P225
BS02 TCL A N139 G140 Y188 Y198 N129 G130 Y178 Y188
Gene Ontology
Molecular Function
GO:0004318 enoyl-[acyl-carrier-protein] reductase (NADH) 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:1d7o, PDBe:1d7o, PDBj:1d7o
PDBsum1d7o
PubMed10610777
UniProtP80030|FABI_BRANA Enoyl-[acyl-carrier-protein] reductase [NADH], chloroplastic

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