Structure of PDB 1cwu Chain B

Receptor sequence
>1cwuB (length=296) Species: 3708 (Brassica napus) [Search protein sequence]
LPIDLRGKRAFIAGIADDNGYGWAVAKSLAAAGAEILVGTWVPALNIFET
SLRRGKFDQSRVLPDGSLMEIKKVYPLDAVFDNPEDVPEDVKANKRYAGS
SNWTVQEAAECVRQDFGSIDILVHSLGNGPEVSKPLLETSRKGYLAAISA
SSYSFVSLLSHFLPIMNPGGASISLTYIASERIIPGYGGGMSSAKAALES
DTRVLAFEAGRKQNIRVNTISAGPLGSRAAKAIGFIDTMIEYSYNNAPIQ
KTLTADEVGNAAAFLVSPLASAITGATIYVDNGLNSMGVALDSPVF
3D structure
PDB1cwu Inhibitor binding studies on enoyl reductase reveal conformational changes related to substrate recognition.
ChainB
Resolution2.5 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) Y187 K195
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 G25 A27 Y32 W52 D89 A90 S136 L137 T187 K206 G234 P235 L236 S238 A240 G14 A16 Y21 W41 D78 A79 S125 L126 T176 K195 G223 P224 L225 S227 A229
BS02 TDB B G138 N139 Y188 Y198 M202 K206 A240 A241 I244 G127 N128 Y177 Y187 M191 K195 A229 A230 I233
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:1cwu, PDBe:1cwu, PDBj:1cwu
PDBsum1cwu
PubMed10521472
UniProtP80030|FABI_BRANA Enoyl-[acyl-carrier-protein] reductase [NADH], chloroplastic

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