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PDBsum entry 2xgi

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protein ligands links
Hydrolase PDB id
2xgi
Jmol
Contents
Protein chain
487 a.a. *
Ligands
EDO ×2
EBG
EBQ
Waters ×741
* Residue conservation analysis
PDB id:
2xgi
Name: Hydrolase
Title: Crystal structure of barley beta-amylase complexed with 3,4- epoxybutyl alpha-d-glucopyranoside
Structure: Beta-amylase. Chain: a. Synonym: 1,4-alpha-d-glucan maltohydrolase. Ec: 3.2.1.2
Source: Hordeum vulgare. Organism_taxid: 4513. Tissue: grain endosperm. Other_details: protein purchased from megazyme
Resolution:
1.30Å     R-factor:   0.129     R-free:   0.157
Authors: M.Rejzek,C.E.M.Stevenson,A.M.Southard,D.Stanley,K.Denyer,A.M M.J.Naldrett,D.M.Lawson,R.A.Field
Key ref: M.Rejzek et al. (2011). Chemical genetics and cereal starch metabolism: structural basis of the non-covalent and covalent inhibition of barley β-amylase. Mol Biosyst, 7, 718-730. PubMed id: 21085740
Date:
04-Jun-10     Release date:   01-Dec-10    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P16098  (AMYB_HORVU) -  Beta-amylase
Seq:
Struc:
 
Seq:
Struc:
535 a.a.
487 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.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     4 terms  

 

 
Mol Biosyst 7:718-730 (2011)
PubMed id: 21085740  
 
 
Chemical genetics and cereal starch metabolism: structural basis of the non-covalent and covalent inhibition of barley β-amylase.
M.Rejzek, C.E.Stevenson, A.M.Southard, D.Stanley, K.Denyer, A.M.Smith, M.J.Naldrett, D.M.Lawson, R.A.Field.
 
  ABSTRACT  
 
No abstract given.