Structure of PDB 6toz Chain A Binding Site BS01

Receptor Information
>6toz Chain A (length=481) Species: 1402 (Bacillus licheniformis) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
LNGTLMQYFEWYMPNDGQHWKRLQNDSAYLAEHGITAVWIPPAYKGTSQD
DVGYGAYDLYDLGEFHQKGTVRTKYGTKGELQSAINSLHSRDINVYGDVV
INHKGGADATEYVTAVEVDPADRNRVTSGEQRIKAWTHFQFPGRGSTYSD
FKWYWYHFDGTDWDESRKLNRIYKFQGKAWDWEVSNENGNYDYLMYADID
YDHPDVTAEIKRWGTWYANELQLDGFRLDAVKHIKFSFLRDWVNHVREKT
GKEMFTVAEYWQNDLGALENYLNKTNFNHSVFDVPLHYQFHAASTQGGGY
DMRKLLNGTVVSKHPVKAVTFVDNHDTQPGQSLESTVQTWFKPLAYAFIL
TREAGYPQIFYGDMYGTKGASQREIPALKHKIEPILKARKQYAYGAQHDY
FDHHNIVGWTREGDSSVANSGLAALITDGPGGTKRMYVGRQNAGETWHDI
TGNRSDSVVINAEGWGEFHVNGGSVSIYVQR
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 chain6toz Chain B Residue 2 [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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PDB6toz Characterization of the starch surface binding site on Bacillus paralicheniformis alpha-amylase.
Resolution1.94 Å
Binding residue
(original residue number in PDB)		E189 K234 L335
Binding residue
(residue number reindexed from 1)		E187 K232 L333
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) R229 D231 E261 H327 D328
Catalytic site (residue number reindexed from 1) R227 D229 E259 H325 D326
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:6toz, PDBe:6toz, PDBj:6toz
PDBsum6toz
PubMed33058974
UniProtI3P686

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