Structure of PDB 2qpu Chain C

Receptor sequence

>2qpuC (length=404) Species: 4513 (Hordeum vulgare)

HQVLFQGFNWESWKQSGGWYNMMMGKVDDIAAAGVTHVWLPPPSHSVSNE
GYMPGRLYDIDASKYGNAAELKSLIGALHGKGVQAIADIVINHRCADYKD
SRGIYCIFEGGTSDGRLDWGPHMICRDDTKYSDGTANLDTGADFAAAPDI
DHLNDRVQRELKEWLLWLKSDLGFDAWRLDFARGYSPEMAKVYIDGTSPS
LAVAEVWDNMATGGDGKPNYDQDAHRQNLVNWVDKVGGAASAGMVFDFTT
KGILNAAVEGELWRLIDPQGKAPGVMGWWPAKAVTFVDNHDTGSTQAMWP
FPSDKVMQGYAYILTHPGIPCIFYDHFFNWGFKDQIAALVAIRKRNGITA
TSALKILMHEGDAYVAEIDGKVVVKIGPRYDVGAVIPAGFVTSAHGNDYA
VWEK

3D structure

• PDB: 2qpu The 'pair of sugar tongs' site on the non-catalytic domain C of barley alpha-amylase participates in substrate binding and activity
• Chain: C
• Resolution: 1.7 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): D180 E205 D291
• Catalytic site (residue number reindexed from 1): 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	CA	C	N92 D139 A142 D149 G184	N92 D139 A142 D149 G184
BS02	CA	C	E109 T112 D114 D118	E109 T112 D114 D118
BS03	CA	C	D128 D143 F144 A147 P148 D149	D128 D143 F144 A147 P148 D149
BS04	QPU	C	K375 Y380 V382 H395 G396 D398 Y399 W402	K375 Y380 V382 H395 G396 D398 Y399 W402

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:2qpu, PDBe:2qpu, PDBj:2qpu
• PDBsum: 2qpu
• PubMed: 17803687
• UniProt: P00693|AMY1_HORVU Alpha-amylase type A isozyme (Gene Name=AMY1.1)