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PDBsum entry 3eqa

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protein ligands links
Hydrolase PDB id
3eqa
Jmol
Contents
Protein chain
458 a.a. *
Ligands
NAG-NAG-BMA-MAN
NAG-NAG-BMA-MAN-
MAN-MAN-MAN-MAN
MAN ×7
TRS
GOL
Waters ×390
* Residue conservation analysis
PDB id:
3eqa
Name: Hydrolase
Title: Catalytic domain of glucoamylase from aspergillus niger comp tris and glycerol
Structure: Glucoamylase. Chain: a. Fragment: catalytic domain (residues 25-494). Synonym: glucan 1,4-alpha-glucosidase. 1,4-alpha-d-glucan glucohydrolase. Other_details: prepared by subtilisin c-terminal cleavage, with tris and glycerol
Source: Aspergillus niger. Organism_taxid: 5061. Other_details: gene glaa
Resolution:
1.90Å     R-factor:   0.184     R-free:   0.229
Authors: J.Lee,M.Paetzel
Key ref: J.Lee and M.Paetzel (2011). Structure of the catalytic domain of glucoamylase from Aspergillus niger. Acta Crystallogr Sect F Struct Biol Cryst Commun, 67, 188-192. PubMed id: 21301084
Date:
30-Sep-08     Release date:   13-Oct-09    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P69328  (AMYG_ASPNG) -  Glucoamylase
Seq:
Struc:
 
Seq:
Struc:
640 a.a.
458 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.3.2.1.3  - Glucan 1,4-alpha-glucosidase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Hydrolysis of terminal 1,4-linked alpha-D-glucose residues successively from non-reducing ends of the chains with release of beta-D-glucose.
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     polysaccharide metabolic process   1 term 
  Biochemical function     catalytic activity     3 terms  

 

 
Acta Crystallogr Sect F Struct Biol Cryst Commun 67:188-192 (2011)
PubMed id: 21301084  
 
 
Structure of the catalytic domain of glucoamylase from Aspergillus niger.
J.Lee, M.Paetzel.
 
  ABSTRACT  
 
No abstract given.