Structure of PDB 6ag0 Chain A Binding Site BS01

Receptor Information
>6ag0 Chain A (length=482) Species: 1422 (Geobacillus stearothermophilus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
PFNGTMMQYFEWYLPDDGTLWTKVANEANNLSSLGITALWLPPAYKGTSR
SDVGYGVYDLYDLGEFNQKGTVRTKYGTKAQYLQAIQAAHAAGMQVYADV
VFDHKGGADGTEWVDAVEVNPSDRNQEISGTYQIQAWTKFDFPGRGNTYS
SFKWRWYHFDGVDWDESRKLSRIYKFRGIGKAWDWEVDTENGNYDYLMYA
DLDMDHPEVVTELKNWGKWYVNTTNIDGFRLDAVKHIKFSFFPDWLSYVR
SQTGKPLFTVGEYWSYDINKLHNYITKTNGTMSLFDAPLHNKFYTASKSG
GAFDMRTLMTNTLMKDQPTLAVTFVDNHDTEPGQALQSWVDPWFKPLAYA
FILTRQEGYPGVFYGDYYGIPQYNIPSLKSKIDPLLIARRDYAYGTQHDY
LDHSDIIGWTREGVTEKPGSGLAALITDGPGGSKWMYVGKQHAGKVFYDL
TGNRSDTVTITSDGWGEFKVNGGSVSVWVPRK
Ligand information
Ligand IDGLC
InChIInChI=1S/C6H12O6/c7-1-2-3(8)4(9)5(10)6(11)12-2/h2-11H,1H2/t2-,3-,4+,5-,6+/m1/s1
InChIKeyWQZGKKKJIJFFOK-DVKNGEFBSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0C(C1C(C(C(C(O1)O)O)O)O)O
OpenEye OEToolkits 1.5.0C([C@@H]1[C@H]([C@@H]([C@H]([C@H](O1)O)O)O)O)O
CACTVS 3.341OC[CH]1O[CH](O)[CH](O)[CH](O)[CH]1O
CACTVS 3.341OC[C@H]1O[C@H](O)[C@H](O)[C@@H](O)[C@@H]1O
ACDLabs 10.04OC1C(O)C(OC(O)C1O)CO
FormulaC6 H12 O6
Namealpha-D-glucopyranose;
alpha-D-glucose;
D-glucose;
glucose
ChEMBLCHEMBL423707
DrugBank
ZINCZINC000003861213
PDB chain6ag0 Chain B Residue 1 [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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PDB6ag0 Crystal structure of a maltooligosaccharide-forming amylase from Bacillus stearothermophilus STB04.
Resolution2.2 Å
Binding residue
(original residue number in PDB)		I181 G182 K183 D205 D207 P209
Binding residue
(residue number reindexed from 1)		I179 G180 K181 D203 D205 P207
Annotation score4
Enzymatic activity
Enzyme Commision number 3.2.1.1: alpha-amylase.
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0004556 alpha-amylase activity
GO:0005509 calcium ion binding
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0046872 metal ion binding
Biological Process
GO:0005975 carbohydrate metabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:6ag0, PDBe:6ag0, PDBj:6ag0
PDBsum6ag0
PubMed31325505
UniProtQ9KWY6

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