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PDBsum entry 2laa

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protein links
Hydrolase PDB id
2laa
Jmol
Contents
Protein chain
104 a.a.
PDB id:
2laa
Name: Hydrolase
Title: Solution strucuture of the cbm25-1 of beta/alpha-amylase fro paenibacillus polymyxa
Structure: Beta/alpha-amylase. Chain: a. Fragment: unp residues 455-558. Synonym: beta-amylase, alpha-amylase. Engineered: yes
Source: Paenibacillus polymyxa. Organism_taxid: 1406. Expressed in: escherichia coli. Expression_system_taxid: 562.
NMR struc: 20 models
Authors: I.Horibe,S.Nishimura,R.Takahashi,T.Ohkubo,T.Yoshida
Key ref: R.Takahashi et al. A functional and structural analysis of tundem family carbohydrate-Binding modules from paenibacillus polym beta/alpha-Amylase. To be published, .
Date:
09-Mar-11     Release date:   04-Apr-12    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P21543  (AMYB_PAEPO) -  Beta/alpha-amylase
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
1196 a.a.
104 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class 2: E.C.3.2.1.1  - Alpha-amylase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Endohydrolysis of 1,4-alpha-glucosidic linkages in oligosaccharides and polysaccharides.
   Enzyme class 3: 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.
Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biochemical function     starch binding     1 term