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PDBsum entry 3a4a

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protein ligands metals links
Hydrolase PDB id
3a4a
Jmol
Contents
Protein chain
586 a.a. *
Ligands
GLC
Metals
_CA
Waters ×582
* Residue conservation analysis
PDB id:
3a4a
Name: Hydrolase
Title: Crystal structure of isomaltase from saccharomyces cerevisia
Structure: Oligo-1,6-glucosidase. Chain: a. Synonym: isomaltase, alpha-glucosidase, flocculent-specific 2. Engineered: yes
Source: Saccharomyces cerevisiae. Yeast. Organism_taxid: 4932. Strain: d-346. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
1.60Å     R-factor:   0.159     R-free:   0.174
Authors: K.Yamamoto,H.Miyake,M.Kusunoki,S.Osaki
Key ref: K.Yamamoto et al. (2010). Crystal structures of isomaltase from Saccharomyces cerevisiae and in complex with its competitive inhibitor maltose. FEBS J, 277, 4205-4214. PubMed id: 20812985
Date:
01-Jul-09     Release date:   14-Jul-10    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P53051  (MALX3_YEAST) -  Oligo-1,6-glucosidase IMA1
Seq:
Struc:
 
Seq:
Struc:
589 a.a.
586 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.3.2.1.10  - Oligo-1,6-glucosidase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Hydrolysis of 1,6-alpha-D-glucosidic linkages in some oligosaccharides produced from starch and glycogen by alpha-amylase, and in isomaltose.
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     mitochondrion   1 term 
  Biological process     metabolic process   4 terms 
  Biochemical function     catalytic activity     6 terms  

 

 
FEBS J 277:4205-4214 (2010)
PubMed id: 20812985  
 
 
Crystal structures of isomaltase from Saccharomyces cerevisiae and in complex with its competitive inhibitor maltose.
K.Yamamoto, H.Miyake, M.Kusunoki, S.Osaki.
 
  ABSTRACT  
 
No abstract given.