Structure of PDB 1edo Chain A

Receptor sequence
>1edoA (length=244) Species: 3708 (Brassica napus) [Search protein sequence]
SPVVVVTGASRGIGKAIALSLGKAGCKVLVNYARSAKAAEEVSKQIEAYG
GQAITFGGDVSKEADVEAMMKTAIDAWGTIDVVVNNAGITRDTLLIRMKK
SQWDEVIDLNLTGVFLCTQAATKIMMKKRKGRIINIASVVGLIGNIGQAN
YAAAKAGVIGFSKTAAREGASRNINVNVVCPGFIASDMTAKLGEDMEKKI
LGTIPLGRTGQPENVAGLVEFLALSPAASYITGQAFTIDGGIAI
3D structure
PDB1edo The X-ray structure of Brassica napus beta-keto acyl carrier protein reductase and its implications for substrate binding and catalysis.
ChainA
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) G28 S154 Y167 K171
Catalytic site (residue number reindexed from 1) G12 S138 Y151 K155
Enzyme Commision number 1.1.1.100: 3-oxoacyl-[acyl-carrier-protein] reductase.
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 NAP A G24 S26 R27 I29 N47 Y48 A49 R50 S51 D75 V76 N102 A103 S154 Y167 K171 P197 G198 I200 S202 M204 G8 S10 R11 I13 N31 Y32 A33 R34 S35 D59 V60 N86 A87 S138 Y151 K155 P181 G182 I184 S186 M188
Gene Ontology
Molecular Function
GO:0004316 3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity
GO:0016491 oxidoreductase activity
GO:0051287 NAD binding
Biological Process
GO:0006633 fatty acid biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:1edo, PDBe:1edo, PDBj:1edo
PDBsum1edo
PubMed10801480
UniProtQ93X62|FABG1_BRANA 3-oxoacyl-[acyl-carrier-protein] reductase 1, chloroplastic (Gene Name=gbkr1)

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