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Receptor Information

>1bg9 Chain A (length=403) Species: 4513 (Hordeum vulgare) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]

QVLFQGFNWESWKHNGGWYNFLMGKVDDIAAAGITHVWLPPASQSVAEQG
YMPGRLYDLDASKYGNKAQLKSLIGALHGKGVKAIADIVINHRTAEHKDG
RGIYCIFEGGTPDARLDWGPHMICRDDRPYADGTGNPDTGADFGAAPDID
HLNLRVQKELVEWLNWLKADIGFDGWRFDFAKGYSADVAKIYIDRSEPSF
AVAEIWTSLAYGGDGKPNLNQDQHRQELVNWVDKVGGKGPATTFDFTTKG
ILNVAVEGELWRLRGTDGKAPGMIGWWPAKAVTFVDNHDTGSTQHMWPFP
SDRVMQGYAYILTHPGTPCIFYDHFFDWGLKEEIDRLVSVRTRHGIHNES
KLQIIEADADLYLAEIDGKVIVKLGPRYDVGNLIPGGFKVAAHGNDYAVW
EKI

Ligand ID

AF1

InChI

InChI=1S/C13H23NO8/c1-4-7(10(18)12(20)13(21)22-4)14-6-2-5(3-15)8(16)11(19)9(6)17/h2,4,6-21H,3H2,1H3/t4-,6+,7-,8?,9+,10+,11+,12-,13-/m1/s1

InChIKey

RBZIIHWPZWOIDU-MKXIPYFISA-N

SMILES

Software	SMILES
OpenEye OEToolkits 1.5.0	CC1C(C(C(C(O1)O)O)O)NC2C=C(C(C(C2O)O)O)CO
OpenEye OEToolkits 1.5.0	CC1[C@H]([C@@H]([C@H]([C@@H](O1)O)O)O)N[C@H]2C=C(C([C@@H]([C@H]2O)O)O)CO
CACTVS 3.341	C[C@H]1O[C@@H](O)[C@H](O)[C@@H](O)[C@@H]1N[C@H]2C=C(CO)[C@H](O)[C@H](O)[C@H]2O
CACTVS 3.341	C[CH]1O[CH](O)[CH](O)[CH](O)[CH]1N[CH]2C=C(CO)[CH](O)[CH](O)[CH]2O
ACDLabs 10.04	OC2C(NC1C=C(CO)C(O)C(O)C1O)C(OC(O)C2O)C

Formula

C13 H23 N O8

Name

4,6-dideoxy-4-{[(1S,4S,5S,6S)-4,5,6-trihydroxy-3-(hydroxymethyl)cyclohex-2-en-1-yl]amino}-beta-D-glucopyranose;
4,6-dideoxy-4-{[(1S,4S,5S,6S)-4,5,6-trihydroxy-3-(hydroxymethyl)cyclohex-2-en-1-yl]amino}-beta-D-glucose;
4,6-dideoxy-4-{[(1S,4S,5S,6S)-4,5,6-trihydroxy-3-(hydroxymethyl)cyclohex-2-en-1-yl]amino}-D-glucose;
4,6-dideoxy-4-{[(1S,4S,5S,6S)-4,5,6-trihydroxy-3-(hydroxymethyl)cyclohex-2-en-1-yl]amino}-glucose

PDB chain

1bg9 Chain A Residue 803 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]

Receptor-Ligand Complex Structure

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Structure summary

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PDB	1bg9 Molecular structure of a barley alpha-amylase-inhibitor complex: implications for starch binding and catalysis.
Resolution	2.8 Å
Binding residue (original residue number in PDB)	Q226 V229 D233 W276 W277
Binding residue (residue number reindexed from 1)	Q226 V229 D233 W276 W277
Annotation score	1

Catalytic site (original residue number in PDB)	D179 E204 D289
Catalytic site (residue number reindexed from 1)	D179 E204 D289
Enzyme Commision number	3.2.1.1: alpha-amylase.

	Molecular Function
GO:0004556	alpha-amylase activity
GO:0005509	calcium ion binding
GO:0016798	hydrolase activity, acting on glycosyl bonds
GO:0043169	cation binding
GO:0046872	metal ion binding

	Biological Process
GO:0005975	carbohydrate metabolic process
GO:0005983	starch catabolic process

PDB	RCSB:1bg9, PDBe:1bg9, PDBj:1bg9
PDBsum	1bg9
PubMed	9571044
UniProt	P04063\|AMY2_HORVU Alpha-amylase type B isozyme (Gene Name=AMY1.2)

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Structure of PDB 1bg9 Chain A Binding Site BS06