PDBsum entry 1j11

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Hydrolase PDB id
Protein chains
516 a.a. *
EPG ×4
_CA ×4
Waters ×526
* Residue conservation analysis
PDB id:
Name: Hydrolase
Title: Beta-amylase from bacillus cereus var. Mycoides in complex with alpha-epg
Structure: Beta-amylase. Chain: a, b, c, d. Synonym: 1,4-alpha-d-glucan maltohydrolase. Ec:
Source: Bacillus cereus. Organism_taxid: 1396. Strain: var. Mycoides
2.00Å     R-factor:   0.200     R-free:   0.246
Authors: T.Oyama,H.Miyake,M.Kusunoki,Y.Nitta
Key ref: T.Oyama et al. (2003). Crystal structures of beta-amylase from Bacillus cereus var mycoides in complexes with substrate analogs and affinity-labeling reagents. J Biochem, 133, 467-474. PubMed id: 12761294
25-Nov-02     Release date:   17-Jun-03    
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Protein chains
Pfam   ArchSchema ?
P36924  (AMYB_BACCE) -  Beta-amylase
546 a.a.
516 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.  - Beta-amylase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Hydrolysis of 1,4-alpha-glucosidic linkages in polysaccharides so as to remove successive maltose units from the non-reducing ends of the chains.
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     metabolic process   4 terms 
  Biochemical function     starch binding     5 terms  


J Biochem 133:467-474 (2003)
PubMed id: 12761294  
Crystal structures of beta-amylase from Bacillus cereus var mycoides in complexes with substrate analogs and affinity-labeling reagents.
T.Oyama, H.Miyake, M.Kusunoki, Y.Nitta.
The crystal structures of beta-amylase from Bacillus cereus var. mycoides in complexes with five inhibitors were solved. The inhibitors used were three substrate analogs, i.e. glucose, maltose (product), and a synthesized compound, O-alpha-D-glucopyranosyl-(1-->4)-O-alpha-D-glucopyranosyl-(1-->4)-D-xylopyranose (GGX), and two affinity-labeling reagents with an epoxy alkyl group at the reducing end of glucose. For all inhibitors, one molecule was bound at the active site cleft and the non-reducing end glucose of the four inhibitors except GGX was located at subsite 1, accompanied by a large conformational change of the flexible loop (residues 93-97), which covered the bound inhibitor. In addition, another molecule of maltose or GGX was bound about 30 A away from the active site. A large movement of residues 330 and 331 around subsite 3 was also observed upon the binding of GGX at subsites 3 to 5. Two affinity-labeling reagents, alpha-EPG and alpha-EBG, were covalently bound to a catalytic residue (Glu-172). A substrate recognition mechanism for the beta-amylase was discussed based on the modes of binding of these inhibitors in the active site cleft.

Literature references that cite this PDB file's key reference

  PubMed id Reference
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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