BioLiP

Receptor Information

>1ose Chain A (length=496) Species: 9823 (Sus scrofa) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]

QYAPQTQSGRTSIVHLFEWRWVDIALECERYLGPKGFGGVQVSPPNENIV
VTNPSRPWWERYQPVSYKLCTRSGNENEFRDMVTRCNNVGVRIYVDAVIN
HMCGSGAAAGTGTTCGSYCNPGSREFPAVPYSAWDFNDGKCKTASGGIES
YNDPYQVRDCQLVGLLDLALEKDYVRSMIADYLNKLIDIGVAGFRIDASK
HMWPGDIKAVLDKLHNLNTNWFPAGSRPFIFQEVIDLGGEAIQSSEYFGN
GRVTEFKYGAKLGTVVRKWSGEKMSYLKNWGEGWGFMPSDRALVFVDNHD
NQRGHGAGGASILTFWDARLYKVAVGFMLAHPYGFTRVMSSYRWARNFVN
GEDVNDWIGPPNNNGVIKEVTINADTTCGNDWVCEHRWREIRNMVWFRNV
VDGEPFANWWDNGSNQVAFGRGNRGFIVFNNDDWQLSSTLQTGLPGGTYC
DVISGDKVGNSCTGIKVYVSSDGTAQFSISNSAEDPFIAIHAESKL

Ligand ID

AC1

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-ZCGMLSCUSA-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
CACTVS 3.341	C[CH]1O[CH](O)[CH](O)[CH](O)[CH]1N[CH]2C=C(CO)[CH](O)[CH](O)[CH]2O
OpenEye OEToolkits 1.5.0	C[C@@H]1[C@H]([C@@H]([C@H]([C@H](O1)O)O)O)N[C@H]2C=C([C@H]([C@@H]([C@H]2O)O)O)CO
ACDLabs 10.04	OC2C(NC1C=C(CO)C(O)C(O)C1O)C(OC(O)C2O)C
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

Formula

C13 H23 N O8

Name

4,6-dideoxy-4-{[(1S,4R,5S,6S)-4,5,6-trihydroxy-3-(hydroxymethyl)cyclohex-2-en-1-yl]amino}-alpha-D-glucopyranose;
6-METHYL-5-(4,5,6-TRIHYDROXY-3-HYDROXYMETHYL-CYCLOHEX-2-ENYLAMINO)-TETRAHYDRO-PYRAN-2,3,4-TRIOL;
4,6-dideoxy-4-{[(1S,4R,5S,6S)-4,5,6-trihydroxy-3-(hydroxymethyl)cyclohex-2-en-1-yl]amino}-alpha-D-glucose;
4,6-dideoxy-4-{[(1S,4R,5S,6S)-4,5,6-trihydroxy-3-(hydroxymethyl)cyclohex-2-en-1-yl]amino}-D-glucose;
4,6-dideoxy-4-{[(1S,4R,5S,6S)-4,5,6-trihydroxy-3-(hydroxymethyl)cyclohex-2-en-1-yl]amino}-glucose

PDB chain

1ose Chain B Residue 4 [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	1ose Crystal structure of pig pancreatic alpha-amylase isoenzyme II, in complex with the carbohydrate inhibitor acarbose.
Resolution	2.3 Å
Binding residue (original residue number in PDB)	W59 S105 G106 V163 G164
Binding residue (residue number reindexed from 1)	W59 S105 G106 V163 G164
Annotation score	1

Catalytic site (original residue number in PDB)	D197 S226 D300
Catalytic site (residue number reindexed from 1)	D197 S226 D300
Enzyme Commision number	3.2.1.1: alpha-amylase.

	Molecular Function
GO:0003824	catalytic activity
GO:0004556	alpha-amylase activity
GO:0005509	calcium ion binding
GO:0016160	amylase activity
GO:0016798	hydrolase activity, acting on glycosyl bonds
GO:0031404	chloride ion binding
GO:0043169	cation binding
GO:0046872	metal ion binding

	Biological Process
GO:0005975	carbohydrate metabolic process
GO:0016052	carbohydrate catabolic process

	Cellular Component
GO:0005576	extracellular region
GO:0005615	extracellular space

PDB	RCSB:1ose, PDBe:1ose, PDBj:1ose
PDBsum	1ose
PubMed	8681972
UniProt	P00690\|AMYP_PIG Pancreatic alpha-amylase (Gene Name=AMY2)

[Back to BioLiP]

Structure of PDB 1ose Chain A Binding Site BS03