Structure of PDB 2qpu Chain B Binding Site BS06

Receptor Information
>2qpu Chain B (length=404) Species: 4513 (Hordeum vulgare) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
HQVLFQGFNWESWKQSGGWYNMMMGKVDDIAAAGVTHVWLPPPSHSVSNE
GYMPGRLYDIDASKYGNAAELKSLIGALHGKGVQAIADIVINHRCADYKD
SRGIYCIFEGGTSDGRLDWGPHMICRDDTKYSDGTANLDTGADFAAAPDI
DHLNDRVQRELKEWLLWLKSDLGFDAWRLDFARGYSPEMAKVYIDGTSPS
LAVAEVWDNMATGGDGKPNYDQDAHRQNLVNWVDKVGGAASAGMVFDFTT
KGILNAAVEGELWRLIDPQGKAPGVMGWWPAKAVTFVDNHDTGSTQAMWP
FPSDKVMQGYAYILTHPGIPCIFYDHFFNWGFKDQIAALVAIRKRNGITA
TSALKILMHEGDAYVAEIDGKVVVKIGPRYDVGAVIPAGFVTSAHGNDYA
VWEK
Ligand information
Ligand IDQPU
InChIInChI=1S/C19H35NO12/c1-5-11(23)10(15(27)16(28)12(5)24)20-9-6(2)31-19(17(29)14(9)26)32-18-8(3-21)30-4-7(22)13(18)25/h5-29H,3-4H2,1-2H3/t5-,6+,7-,8+,9+,10-,11+,12+,13+,14-,15-,16-,17+,18+,19+/m0/s1
InChIKeyNJMZSGBZXMLUCS-JMXNYNASSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04O(C1C(OCC(O)C1O)CO)C3OC(C(NC2C(O)C(C)C(O)C(O)C2O)C(O)C3O)C
CACTVS 3.341C[C@H]1O[C@H](O[C@H]2[C@H](O)[C@@H](O)CO[C@@H]2CO)[C@H](O)[C@@H](O)[C@@H]1N[C@H]3[C@H](O)[C@H](C)[C@@H](O)[C@H](O)[C@H]3O
OpenEye OEToolkits 1.5.0CC1C(C(C(C(C1O)O)O)NC2C(OC(C(C2O)O)OC3C(OCC(C3O)O)CO)C)O
OpenEye OEToolkits 1.5.0CC1[C@H]([C@@H]([C@@H]([C@H]([C@@H]1O)O)O)N[C@@H]2[C@H](O[C@@H]([C@@H]([C@H]2O)O)O[C@@H]3[C@H](OC[C@@H]([C@H]3O)O)CO)C)O
CACTVS 3.341C[CH]1O[CH](O[CH]2[CH](O)[CH](O)CO[CH]2CO)[CH](O)[CH](O)[CH]1N[CH]3[CH](O)[CH](C)[CH](O)[CH](O)[CH]3O
FormulaC19 H35 N O12
Name1,5-anhydro-4-O-(4,6-dideoxy-4-{[(1S,2S,3S,4R,5S,6R)-2,3,4,6-tetrahydroxy-5-methylcyclohexyl]amino}-alpha-D-glucopyranosyl)-D-glucitol
ChEMBL
DrugBank
ZINCZINC000064497509
PDB chain2qpu Chain B Residue 4000 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB2qpu The 'pair of sugar tongs' site on the non-catalytic domain C of barley alpha-amylase participates in substrate binding and activity
Resolution1.7 Å
Binding residue
(original residue number in PDB)		Q227 V230 D234 W278 W279
Binding residue
(residue number reindexed from 1)		Q227 V230 D234 W278 W279
Annotation score1
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.
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:2qpu, PDBe:2qpu, PDBj:2qpu
PDBsum2qpu
PubMed17803687
UniProtP00693|AMY1_HORVU Alpha-amylase type A isozyme (Gene Name=AMY1.1)

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