Structure of PDB 1ava Chain A

Receptor sequence

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

QVLFQGFNWESWKHNGGWYNFLMGKVDDIAAAGITHVWLPPASQSVAEQG
YMPGRLYDLDASKYGNKAQLKSLIGALHGKGVKAIADIVINHRTAEHKDG
RGIYCIFEGGTPDARLDWGPHMICRDDRPYADGTGNPDTGADFGAAPDID
HLNLRVQKELVEWLNWLKADIGFDGWRFDFAKGYSADVAKIYIDRSEPSF
AVAEIWTSLAYGGDGKPNLNQDQHRQELVNWVDKVGGKGPATTFDFTTKG
ILNVAVEGELWRLRGTDGKAPGMIGWWPAKAVTFVDNHDTGSTQHMWPFP
SDRVMQGYAYILTHPGTPCIFYDHFFDWGLKEEIDRLVSVRTRHGIHNES
KLQIIEADADLYLAEIDGKVIVKLGPRYDVGNLIPGGFKVAAHGNDYAVW
EKI

3D structure

• PDB: 1ava Barley alpha-amylase bound to its endogenous protein inhibitor BASI: crystal structure of the complex at 1.9 A resolution.
• Chain: A
• Resolution: 1.9 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	CA	A	N91 D138 A141 D148 G183	N91 D138 A141 D148 G183
BS02	CA	A	E108 T111 D113 D117	E108 T111 D113 D117
BS03	CA	A	D127 D142 F143 A146 P147 D148	D127 D142 F143 A146 P147 D148

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:1ava, PDBe:1ava, PDBj:1ava
• PDBsum: 1ava
• PubMed: 9634702
• UniProt: P04063|AMY2_HORVU Alpha-amylase type B isozyme (Gene Name=AMY1.2)