Structure of PDB 3bsh Chain A

Receptor sequence

>3bshA (length=404) Species: 4513 (Hordeum vulgare)

HQVLFQGFNWESWKQSGGWYNMMMGKVDDIAAAGVTHVWLPPPSHSVSNE
GYMPGRLYDIDASKYGNAAELKSLIGALHGKGVQAIADIVINHRCADYKD
SRGIACIFEGGTSDGRLDWGPHMICRDDTKYSDGTANLDTGADFAAAPDI
DHLNDRVQRELKEWLLWLKSDLGFDAWRLDFARGYSPEMAKVYIDGTSPS
LAVAEVWDNMATGGDGKPNYDQDAHRQNLVNWVDKVGGAASAGMVFDFTT
KGILNAAVEGELWRLIDPQGKAPGVMGWWPAKAVTFVDNHDTGSTQAMWP
FPSDKVMQGYAYILTHPGIPCIFYDHFFNWGFKDQIAALVAIRKRNGITA
TSALKILMHEGDAYVAEIDGKVVVKIGSRADVGAVIPAGFVTSAHGNDYA
VWEK

3D structure

• PDB: 3bsh Multi-site substrate binding and interplay in barley alpha-amylase 1
• Chain: A
• Resolution: 3.0 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): R178 D180 E205 D291
• Catalytic site (residue number reindexed from 1): R178 D180 E205 D291
• 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	F144 D180 E205 D291	F144 D180 E205 D291
BS02	CA	A	N92 D139 G141 A142 D149 G184	N92 D139 G141 A142 D149 G184
BS03	CA	A	E109 T112 D114 D118	E109 T112 D114 D118
BS04	CA	A	D128 D143 F144 A147 D149	D128 D143 F144 A147 D149

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

Cellular Component

• GO:0005576 extracellular region

External links

• PDB: RCSB:3bsh, PDBe:3bsh, PDBj:3bsh
• PDBsum: 3bsh
• PubMed: 18588886
• UniProt: P00693|AMY1_HORVU Alpha-amylase type A isozyme (Gene Name=AMY1.1)