PDBsum entry 1btc

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Hydrolase(o-glycosyl) PDB id
Protein chain
491 a.a. *
BME ×4
Waters ×318
* Residue conservation analysis
PDB id:
Name: Hydrolase(o-glycosyl)
Title: Three-dimensional structure of soybean beta-amylase determined at 3.0 angstroms resolution: preliminary chain tracing of the complex with alpha-cyclodextrin
Structure: Beta-amylase. Chain: a. Engineered: yes
Source: Glycine max. Soybean. Organism_taxid: 3847
2.00Å     R-factor:   0.177    
Authors: B.Mikami,E.J.Hehre,M.Sato,Y.Katsube,M.Hirose,Y.Morita, J.C.Sacchettini
Key ref: B.Mikami et al. (1992). Three-dimensional structure of soybean beta-amylase determined at 3.0 A resolution: preliminary chain tracing of the complex with alpha-cyclodextrin. J Biochem, 112, 541-546. PubMed id: 1491009
18-Feb-93     Release date:   31-Oct-93    
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Protein chain
Pfam   ArchSchema ?
P10538  (AMYB_SOYBN) -  Beta-amylase
496 a.a.
491 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   3 terms 
  Biochemical function     hydrolase activity     3 terms  


J Biochem 112:541-546 (1992)
PubMed id: 1491009  
Three-dimensional structure of soybean beta-amylase determined at 3.0 A resolution: preliminary chain tracing of the complex with alpha-cyclodextrin.
B.Mikami, M.Sato, T.Shibata, M.Hirose, S.Aibara, Y.Katsube, Y.Morita.
The three-dimensional structure of a complex of soybean beta-amylase [EC] with an inhibitor, alpha-cyclodextrin, has been determined at 3.0 A resolution by X-ray diffraction analysis. Preliminary chain tracing showed that the enzyme folded into large and small domains. The large domain has a (beta alpha)8 super-secondary structure, while the smaller one is formed from two long loops extending from the beta 3 and beta 4 strands of the (beta alpha)8 structure. The interface of the two domains together with shorter loops from the (beta alpha)8 structure form a deep cleft, in which alpha-cyclodextrin binds slightly away from the center. Two maltose molecules also bind in the cleft. One shares a binding site with alpha-cyclodextrin and the other is situated more deeply in the cleft.

Literature references that cite this PDB file's key reference

  PubMed id Reference
  10548053 N.Nagano, E.G.Hutchinson, and J.M.Thornton (1999).
Barrel structures in proteins: automatic identification and classification including a sequence analysis of TIM barrels.
  Protein Sci, 8, 2072-2084.  
  9521098 S.Jones, M.Stewart, A.Michie, M.B.Swindells, C.Orengo, and J.M.Thornton (1998).
Domain assignment for protein structures using a consensus approach: characterization and analysis.
  Protein Sci, 7, 233-242.  
7777485 C.G.Cheong, S.H.Eom, C.Chang, D.H.Shin, H.K.Song, K.Min, J.H.Moon, K.K.Kim, K.Y.Hwang, and S.W.Suh (1995).
Crystallization, molecular replacement solution, and refinement of tetrameric beta-amylase from sweet potato.
  Proteins, 21, 105-117.
PDB code: 1fa2
8710828 T.Madej, J.F.Gibrat, and S.H.Bryant (1995).
Threading a database of protein cores.
  Proteins, 23, 356-369.  
8136030 H.M.Jespersen, E.A.MacGregor, B.Henrissat, M.R.Sierks, and B.Svensson (1993).
Starch- and glycogen-debranching and branching enzymes: prediction of structural features of the catalytic (beta/alpha)8-barrel domain and evolutionary relationship to other amylolytic enzymes.
  J Protein Chem, 12, 791-805.  
8141995 S.Janecek, and S.Baláz (1993).
Evolution of parallel beta/alpha-barrel enzyme family lightened by structural data on starch-processing enzymes.
  J Protein Chem, 12, 509-514.  
  8434930 T.Nanmori, M.Nagai, Y.Shimizu, R.Shinke, and B.Mikami (1993).
Cloning of the beta-amylase gene from Bacillus cereus and characteristics of the primary structure of the enzyme.
  Appl Environ Microbiol, 59, 623-627.  
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