PDBsum entry 3bh4

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protein metals Protein-protein interface(s) links
Hydrolase PDB id
Protein chains
483 a.a. *
_NA ×2
_CA ×8
Waters ×647
* Residue conservation analysis
PDB id:
Name: Hydrolase
Title: High resolution crystal structure of bacillus amyloliquefaciens alpha-amylase
Structure: Alpha-amylase. Chain: a, b. Synonym: 1,4-alpha-d-glucan glucanohydrolase. Engineered: yes
Source: Bacillus amyloliquefaciens. Organism_taxid: 1390
1.40Å     R-factor:   0.206     R-free:   0.219
Authors: J.Alikhajeh,K.Khajeh,B.Ranjbar,H.Naderi-Manesh,Y.H.Lin, M.Y.Liu,C.J.Chen
Key ref: J.Alikhajeh et al. (2010). Structure of Bacillus amyloliquefaciens alpha-amylase at high resolution: implications for thermal stability. Acta Crystallogr Sect F Struct Biol Cryst Commun, 66, 121-129. PubMed id: 20124706
28-Nov-07     Release date:   09-Dec-08    
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Protein chains
Pfam   ArchSchema ?
P00692  (AMY_BACAM) -  Alpha-amylase
514 a.a.
483 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 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   1 term 
  Biological process     metabolic process   2 terms 
  Biochemical function     catalytic activity     8 terms  


Acta Crystallogr Sect F Struct Biol Cryst Commun 66:121-129 (2010)
PubMed id: 20124706  
Structure of Bacillus amyloliquefaciens alpha-amylase at high resolution: implications for thermal stability.
J.Alikhajeh, K.Khajeh, B.Ranjbar, H.Naderi-Manesh, Y.H.Lin, E.Liu, H.H.Guan, Y.C.Hsieh, P.Chuankhayan, Y.C.Huang, J.Jeyaraman, M.Y.Liu, C.J.Chen.
The crystal structure of Bacillus amyloliquefaciens alpha-amylase (BAA) at 1.4 A resolution revealed ambiguities in the thermal adaptation of homologous proteins in this family. The final model of BAA is composed of two molecules in a back-to-back orientation, which is likely to be a consequence of crystal packing. Despite a high degree of identity, comparison of the structure of BAA with those of other liquefying-type alpha-amylases indicated moderate discrepancies at the secondary-structural level. Moreover, a domain-displacement survey using anisotropic B-factor and domain-motion analyses implied a significant contribution of domain B to the total flexibility of BAA, while visual inspection of the structure superimposed with that of B. licheniformis alpha-amylase (BLA) indicated higher flexibility of the latter in the central domain A. Therefore, it is suggested that domain B may play an important role in liquefying alpha-amylases, as its rigidity offers a substantial improvement in thermostability in BLA compared with BAA.