Structure of PDB 2qps Chain A

Receptor sequence
>2qpsA (length=404) Species: 4513 (Hordeum vulgare) [Search protein sequence]
HQVLFQGFNWESWKQSGGWYNMMMGKVDDIAAAGVTHVWLPPPSHSVSNE
GYMPGRLYDIDASKYGNAAELKSLIGALHGKGVQAIADIVINHRCADYKD
SRGIYCIFEGGTSDGRLDWGPHMICRDDTKYSDGTANLDTGADFAAAPDI
DHLNDRVQRELKEWLLWLKSDLGFDAWRLDFARGYSPEMAKVYIDGTSPS
LAVAEVWDNMATGGDGKPNYDQDAHRQNLVNWVDKVGGAASAGMVFDFTT
KGILNAAVEGELWRLIDPQGKAPGVMGWWPAKAVTFVDNHDTGSTQAMWP
FPSDKVMQGYAYILTHPGIPCIFYDHFFNWGFKDQIAALVAIRKRNGITA
TSALKILMHEGDAYVAEIDGKVVVKIGSRADVGAVIPAGFVTSAHGNDYA
VWEK
3D structure
PDB2qps The 'pair of sugar tongs' site on the non-catalytic domain C of barley alpha-amylase participates in substrate binding and activity
ChainA
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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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 A N92 D139 G141 A142 D149 G184 N92 D139 G141 A142 D149 G184
BS02 CA A E109 T112 S113 D114 D118 E109 T112 S113 D114 D118
BS03 CA A D128 D143 F144 A147 P148 D149 D128 D143 F144 A147 P148 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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2qps, PDBe:2qps, PDBj:2qps
PDBsum2qps
PubMed17803687
UniProtP00693|AMY1_HORVU Alpha-amylase type A isozyme (Gene Name=AMY1.1)

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