PDBsum entry 3bsh

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Hydrolase PDB id
Protein chain
404 a.a. *
_CA ×3
Waters ×112
* Residue conservation analysis
PDB id:
Name: Hydrolase
Title: Barley alpha-amylase isozyme 1 (amy1) double mutant y105a/y380a in complex with inhibitor acarbose
Structure: Alpha-amylase type a isozyme. Chain: a. Synonym: alpha-amylase isozyme 1, 1,4-alpha-d- glucan glucanohydrolase, amy1, low pi alpha-amylase. Engineered: yes. Mutation: yes
Source: Hordeum vulgare. Barley. Organism_taxid: 4513. Expressed in: pichia pastoris. Expression_system_taxid: 4922.
3.00Å     R-factor:   0.197     R-free:   0.268
Authors: N.Aghajari,X.Robert,R.Haser
Key ref: M.M.Nielsen et al. (2008). Multi-site substrate binding and interplay in barley alpha-amylase 1. FEBS Lett, 582, 2567-2571. PubMed id: 18588886 DOI: 10.1016/j.febslet.2008.06.027
24-Dec-07     Release date:   26-Aug-08    
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
P00693  (AMY1_HORVU) -  Alpha-amylase type A isozyme
438 a.a.
404 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 3 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: E.C.  - Alpha-amylase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Endohydrolysis of 1,4-alpha-glucosidic linkages in oligosaccharides and polysaccharides.
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     extracellular region   2 terms 
  Biological process     metabolic process   4 terms 
  Biochemical function     catalytic activity     7 terms  


DOI no: 10.1016/j.febslet.2008.06.027 FEBS Lett 582:2567-2571 (2008)
PubMed id: 18588886  
Multi-site substrate binding and interplay in barley alpha-amylase 1.
M.M.Nielsen, E.S.Seo, S.Bozonnet, N.Aghajari, X.Robert, R.Haser, B.Svensson.
Certain starch hydrolases possess secondary carbohydrate binding sites outside of the active site, suggesting that multi-site substrate interactions are functionally significant. In barley alpha-amylase both Tyr380, situated on a remote non-catalytic domain, and Tyr105 in subsite -6 of the active site cleft are principal carbohydrate binding residues. The dual active site/secondary site mutants Y105A/Y380A and Y105A/Y380M show that each of Tyr380 and Tyr105 is important, albeit not essential for binding, degradation, and multiple attack on polysaccharides, while Tyr105 predominates in oligosaccharide hydrolysis. Additional delicate structure/function relationships of the secondary site are uncovered using Y380A/H395A, Y380A, and H395A AMY1 mutants.

Literature references that cite this PDB file's key reference

  PubMed id Reference
20017116 R.L.Rich, and D.G.Myszka (2010).
Grading the commercial optical biosensor literature-Class of 2008: 'The Mighty Binders'.
  J Mol Recognit, 23, 1.  
19682075 C.Christiansen, M.Abou Hachem, S.Janecek, A.Viksø-Nielsen, A.Blennow, and B.Svensson (2009).
The carbohydrate-binding module family 20--diversity, structure, and function.
  FEBS J, 276, 5006-5029.  
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