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PDBsum entry 1ua7

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protein ligands metals links
Hydrolase PDB id
1ua7
Jmol
Contents
Protein chain
422 a.a. *
Ligands
ACI-GLD-GLC-ACI-
G6D-BGC
Metals
_CA ×3
Waters ×437
* Residue conservation analysis
PDB id:
1ua7
Name: Hydrolase
Title: Crystal structure analysis of alpha-amylase from bacillus subtilis complexed with acarbose
Structure: Alpha-amylase. Chain: a. Fragment: residues 4-425. Synonym: alpha-1,4-glucan-4-glucanohydrolase. Engineered: yes. Mutation: yes
Source: Bacillus subtilis. Organism_taxid: 1423. Expressed in: bacillus subtilis. Expression_system_taxid: 1423.
Resolution:
2.21Å     R-factor:   0.208     R-free:   0.265
Authors: M.Kagawa,Z.Fujimoto,M.Momma,K.Takase,H.Mizuno
Key ref: M.Kagawa et al. (2003). Crystal structure of Bacillus subtilis alpha-amylase in complex with acarbose. J Bacteriol, 185, 6981-6984. PubMed id: 14617662
Date:
03-Mar-03     Release date:   18-May-04    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P00691  (AMY_BACSU) -  Alpha-amylase
Seq:
Struc:
 
Seq:
Struc:
659 a.a.
422 a.a.*
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 3 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: E.C.3.2.1.1  - 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!
  Biological process     carbohydrate metabolic process   1 term 
  Biochemical function     catalytic activity     2 terms  

 

 
J Bacteriol 185:6981-6984 (2003)
PubMed id: 14617662  
 
 
Crystal structure of Bacillus subtilis alpha-amylase in complex with acarbose.
M.Kagawa, Z.Fujimoto, M.Momma, K.Takase, H.Mizuno.
 
  ABSTRACT  
 
The crystal structure of Bacillus subtilis alpha-amylase, in complex with the pseudotetrasaccharide inhibitor acarbose, revealed an hexasaccharide in the active site as a result of transglycosylation. After comparison with the known structure of the catalytic-site mutant complexed with the native substrate maltopentaose, it is suggested that the present structure represents a mimic intermediate in the initial stage of the catalytic process.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
19756583 F.M.Reyes-Sosa, F.P.Molina-Heredia, and M.A.De la Rosa (2010).
A novel alpha-amylase from the cyanobacterium Nostoc sp. PCC 7119.
  Appl Microbiol Biotechnol, 86, 131-141.  
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.