Structure of PDB 1bg9 Chain A

Receptor sequence

>1bg9A (length=403) Species: 4513 (Hordeum vulgare)

QVLFQGFNWESWKHNGGWYNFLMGKVDDIAAAGITHVWLPPASQSVAEQG
YMPGRLYDLDASKYGNKAQLKSLIGALHGKGVKAIADIVINHRTAEHKDG
RGIYCIFEGGTPDARLDWGPHMICRDDRPYADGTGNPDTGADFGAAPDID
HLNLRVQKELVEWLNWLKADIGFDGWRFDFAKGYSADVAKIYIDRSEPSF
AVAEIWTSLAYGGDGKPNLNQDQHRQELVNWVDKVGGKGPATTFDFTTKG
ILNVAVEGELWRLRGTDGKAPGMIGWWPAKAVTFVDNHDTGSTQHMWPFP
SDRVMQGYAYILTHPGTPCIFYDHFFDWGLKEEIDRLVSVRTRHGIHNES
KLQIIEADADLYLAEIDGKVIVKLGPRYDVGNLIPGGFKVAAHGNDYAVW
EKI

3D structure

• PDB: 1bg9 Molecular structure of a barley alpha-amylase-inhibitor complex: implications for starch binding and catalysis.
• Chain: A
• Resolution: 2.8 Å

Enzymatic activity

• 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.

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	BGC	A	W206 S208 M296	W206 S208 M296
BS02	DAF	A	Y51 H92 F143 R177 D179 F180 E204 H288 D289 M296	Y51 H92 F143 R177 D179 F180 E204 H288 D289 M296
BS03	CA	A	N91 D138 G140 A141 D148 G183	N91 D138 G140 A141 D148 G183
BS04	CA	A	E108 T111 D113 D117	E108 T111 D113 D117
BS05	CA	A	D127 D142 F143 A146 D148	D127 D142 F143 A146 D148
BS06	AF1	A	Q226 V229 D233 W276 W277	Q226 V229 D233 W276 W277

Gene Ontology

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

External links

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