Structure of PDB 1bli Chain A

Receptor sequence

>1bliA (length=481) Species: 1402 (Bacillus licheniformis)

LNGTLMQYFEWYMPNDGQHWKRLQNDSAYLAEHGITAVWIPPAYKGTSQA
DVGYGAYDLYDLGEFHQKGTVRTKYGTKGELQSAIKSLHSRDINVYGDVV
INHKGGADATEDVTAVEVDPADRNRVISGEHLIKAWTHFHFPGRGSTYSD
FKWHWYHFDGTDWDESRKLNRIYKFQGKAWDWEVSNEFGNYDYLMYADID
YDHPDVAAEIKRWGTWYANELQLDGFRLDAVKHIKFSFLRDWVNHVREKT
GKEMFTVAEYWSYDLGALENYLNKTNFNHSVFDVPLHYQFHAASTQGGGY
DMRKLLNGTVVSKHPLKSVTFVDNHDTQPGQSLESTVQTWFKPLAYAFIL
TRESGYPQVFYGDMYGTKGDSQREIPALKHKIEPILKARKQYAYGAQHDY
FDHHDIVGWTREGDSSVANSGLAALITDGPGGAKRMYVGRQNAGETWHDI
TGNRSEPVVINSAGWGEFHVNGGSVSIYVQR

3D structure

• PDB: 1bli Activation of Bacillus licheniformis alpha-amylase through a disorder-->order transition of the substrate-binding site mediated by a calcium-sodium-calcium metal triad.
• Chain: A
• Resolution: 1.9 Å

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.

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	CA	A	D161 A181 D183 D202 D204	D159 A179 D181 D200 D202
BS02	CA	A	N104 D194 D200 H235	N102 D192 D198 H233
BS03	CA	A	G300 Y302 H406 D407 D430	G298 Y300 H404 D405 D428
BS04	NA	A	D161 D183 D194 D200 I201 D202	D159 D181 D192 D198 I199 D200

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

External links

• PDB: RCSB:1bli, PDBe:1bli, PDBj:1bli
• PDBsum: 1bli
• PubMed: 9551551
• UniProt: P06278|AMY_BACLI Alpha-amylase (Gene Name=amyS)