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PDBsum entry 1btc

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protein ligands links
Hydrolase(o-glycosyl) PDB id
1btc
Jmol
Contents
Protein chain
491 a.a. *
Ligands
GLC-GLC-GLC-GLC-
GLC-GLC
SO4
BME ×4
Waters ×318
* Residue conservation analysis
PDB id:
1btc
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
Resolution:
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
Date:
18-Feb-93     Release date:   31-Oct-93    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P10538  (AMYB_SOYBN) -  Beta-amylase
Seq:
Struc:
496 a.a.
491 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.3.2.1.2  - 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.
 
  ABSTRACT  
 
The three-dimensional structure of a complex of soybean beta-amylase [EC 3.2.1.2] 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.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.