Structure of PDB 5a2b Chain A Binding Site BS01

Receptor Information
>5a2b Chain A (length=452) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
ERTWQDERIYFIMVDRFNNGNPKNDYEVDVHDPKAYHGGDLQGIIDKLDY
IKEMGFTAIWLTPIFANEKGGYHGYWIEDFYKVEEHFGTLDDFKRLVKEA
HKRDMKVILDFVVNHTGYNHPWLNDPAKKDWFHEKKDIFNWANQQEVENG
WLFGLPDLAQENPEVKTYLFDVAKWWIQETDIDGYRLDTVKHVPKWFWDE
FAKEVKSVKQDFFLLGEVWHDDPRYVAEYGKHGIDALIDFPFYKEASTIF
SNVDQSLEPLYNVWKRNVAFYERPYLLGTFLDNHDTVRFTRLALQNRINP
VTRLKLGLTYLFSAPGIPIMYYGTEIALDGGEDPDNRRLMNFRTDKELID
YVTKLGELRAKLPSLRRGDFELLYEKDGMALFKRTYEKETTVIAINNTSK
TQKVTLDGELEQGKELRGLLAGDLVRSKDGKYDIILDRETAEIYVLAPKT
GL
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 chain5a2b 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

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB5a2b Crystal Structure of Anoxybacillus Alpha-Amylase Provides Insights Into Maltose Binding of a New Glycosyl Hydrolase Subclass.
Resolution1.85 Å
Binding residue
(original residue number in PDB)		Y100 H140 D213 T214 E242 H309 D310
Binding residue
(residue number reindexed from 1)		Y75 H115 D188 T189 E217 H284 D285
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) D135 R211 D213 E242 H309 D310
Catalytic site (residue number reindexed from 1) D110 R186 D188 E217 H284 D285
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:0046872 metal ion binding
Biological Process
GO:0005975 carbohydrate metabolic process
Cellular Component
GO:0016020 membrane

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:5a2b, PDBe:5a2b, PDBj:5a2b
PDBsum5a2b
PubMed26975884
UniProtI1VWH9

[Back to BioLiP]