BioLiP

Receptor Information

>1edo Chain A (length=244) Species: 3708 (Brassica napus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]

SPVVVVTGASRGIGKAIALSLGKAGCKVLVNYARSAKAAEEVSKQIEAYG
GQAITFGGDVSKEADVEAMMKTAIDAWGTIDVVVNNAGITRDTLLIRMKK
SQWDEVIDLNLTGVFLCTQAATKIMMKKRKGRIINIASVVGLIGNIGQAN
YAAAKAGVIGFSKTAAREGASRNINVNVVCPGFIASDMTAKLGEDMEKKI
LGTIPLGRTGQPENVAGLVEFLALSPAASYITGQAFTIDGGIAI

Ligand ID

NAP

InChI

InChI=1S/C21H28N7O17P3/c22-17-12-19(25-7-24-17)28(8-26-12)21-16(44-46(33,34)35)14(30)11(43-21)6-41-48(38,39)45-47(36,37)40-5-10-13(29)15(31)20(42-10)27-3-1-2-9(4-27)18(23)32/h1-4,7-8,10-11,13-16,20-21,29-31H,5-6H2,(H7-,22,23,24,25,32,33,34,35,36,37,38,39)/t10-,11-,13-,14-,15-,16-,20-,21-/m1/s1

InChIKey

XJLXINKUBYWONI-NNYOXOHSSA-N

SMILES

Software	SMILES
OpenEye OEToolkits 1.5.0	c1cc(c[n+](c1)C2C(C(C(O2)COP(=O)([O-])OP(=O)(O)OCC3C(C(C(O3)n4cnc5c4ncnc5N)OP(=O)(O)O)O)O)O)C(=O)N
CACTVS 3.341	NC(=O)c1ccc[n+](c1)[CH]2O[CH](CO[P]([O-])(=O)O[P](O)(=O)OC[CH]3O[CH]([CH](O[P](O)(O)=O)[CH]3O)n4cnc5c(N)ncnc45)[CH](O)[CH]2O
CACTVS 3.341	NC(=O)c1ccc[n+](c1)[C@@H]2O[C@H](CO[P]([O-])(=O)O[P@@](O)(=O)OC[C@H]3O[C@H]([C@H](O[P](O)(O)=O)[C@@H]3O)n4cnc5c(N)ncnc45)[C@@H](O)[C@H]2O
OpenEye OEToolkits 1.5.0	c1cc(c[n+](c1)[C@H]2[C@@H]([C@@H]([C@H](O2)CO[P@@](=O)([O-])O[P@](=O)(O)OC[C@@H]3[C@H]([C@H]([C@@H](O3)n4cnc5c4ncnc5N)OP(=O)(O)O)O)O)O)C(=O)N

Formula

C21 H28 N7 O17 P3

Name

NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE;
2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE

PDB chain

1edo Chain A Residue 301 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]

Receptor-Ligand Complex Structure

Global view

Local view

Structure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]

PDB	1edo The X-ray structure of Brassica napus beta-keto acyl carrier protein reductase and its implications for substrate binding and catalysis.
Resolution	2.3 Å
Binding residue (original residue number in PDB)	G24 S26 R27 I29 N47 Y48 A49 R50 S51 D75 V76 N102 A103 S154 Y167 K171 P197 G198 I200 S202 M204
Binding residue (residue number reindexed from 1)	G8 S10 R11 I13 N31 Y32 A33 R34 S35 D59 V60 N86 A87 S138 Y151 K155 P181 G182 I184 S186 M188
Annotation score	4

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.

	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

PDB	RCSB:1edo, PDBe:1edo, PDBj:1edo
PDBsum	1edo
PubMed	10801480
UniProt	Q93X62\|FABG1_BRANA 3-oxoacyl-[acyl-carrier-protein] reductase 1, chloroplastic (Gene Name=gbkr1)

[Back to BioLiP]

Structure of PDB 1edo Chain A Binding Site BS01