Structure of PDB 1bli Chain A Binding Site BS04

Receptor Information
>1bli 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]
LNGTLMQYFEWYMPNDGQHWKRLQNDSAYLAEHGITAVWIPPAYKGTSQA
DVGYGAYDLYDLGEFHQKGTVRTKYGTKGELQSAIKSLHSRDINVYGDVV
INHKGGADATEDVTAVEVDPADRNRVISGEHLIKAWTHFHFPGRGSTYSD
FKWHWYHFDGTDWDESRKLNRIYKFQGKAWDWEVSNEFGNYDYLMYADID
YDHPDVAAEIKRWGTWYANELQLDGFRLDAVKHIKFSFLRDWVNHVREKT
GKEMFTVAEYWSYDLGALENYLNKTNFNHSVFDVPLHYQFHAASTQGGGY
DMRKLLNGTVVSKHPLKSVTFVDNHDTQPGQSLESTVQTWFKPLAYAFIL
TRESGYPQVFYGDMYGTKGDSQREIPALKHKIEPILKARKQYAYGAQHDY
FDHHDIVGWTREGDSSVANSGLAALITDGPGGAKRMYVGRQNAGETWHDI
TGNRSEPVVINSAGWGEFHVNGGSVSIYVQR
Ligand information
Ligand IDNA
InChIInChI=1S/Na/q+1
InChIKeyFKNQFGJONOIPTF-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
CACTVS 3.341
OpenEye OEToolkits 1.5.0		[Na+]
FormulaNa
NameSODIUM ION
ChEMBL
DrugBankDB14516
ZINC
PDB chain1bli Chain A Residue 800 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1bli Activation of Bacillus licheniformis alpha-amylase through a disorder-->order transition of the substrate-binding site mediated by a calcium-sodium-calcium metal triad.
Resolution1.9 Å
Binding residue
(original residue number in PDB)		D161 D183 D194 D200 I201 D202
Binding residue
(residue number reindexed from 1)		D159 D181 D192 D198 I199 D200
Annotation score3
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
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:1bli, PDBe:1bli, PDBj:1bli
PDBsum1bli
PubMed9551551
UniProtP06278|AMY_BACLI Alpha-amylase (Gene Name=amyS)

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