Brand  (β version)

  The number of atoms exceeds 100,000.
  So, it can not be displayed here.

Select unit:

Select hetatm:   

close
information
centroid:
interaction residue:

Select chain:   Sequence  

Data format:   

Color scheme of protein:

Ligands
Code Name Style Show Link
TRS 2-amino-2-hydroxymethyl-propane-1,3-diol
Non-standard Residues
Code Name Show
Glycosylation
Code Name Emphasize
Modification
Code Name Show
Code : 1AYX   PDBj   RCSB PDB   PDBe
Header : HYDROLASE
Title : CRYSTAL STRUCTURE OF GLUCOAMYLASE FROM SACCHAROMYCOPSIS FIBULIGERA AT 1.7 ANGSTROMS
Release Data : 1998-05-13
Compound :
mol_id molecule chains
1 GLUCOAMYLASE A
ec: 3.2.1.3
Source :
mol_id organism_scientific expression_system
1 Saccharomycopsis fibuligera  (taxid:4944) Escherichia coli  (taxid:562)
gene: GLU1
Authors : Sevcik, J., Hostinova, E., Gasperik, J., Solovicova, A., Wilson, K.S., Dauter, Z.
Keywords : GLUCOAMYLASE, HYDROLASE, GLYCOSIDASE, POLYSACCHARIDE DEGRADATION
Exp. method : X-RAY DIFFRACTION ( 1.70 Å )
Citation :

Structure of glucoamylase from Saccharomycopsis fibuligera at 1.7 A resolution.

Sevcik, J.,Solovicova, A.,Hostinova, E.  et al.
(1998)  Acta Crystallogr.,Sect.D  54 : 854 - 866

PubMed: 9757101
DOI: 10.1107/S0907444998002005

Chain : A
UniProt : P08017 (AMYG_SACFI)
Reaction: EC: Evidence:
Physiological Direction:
Hydrolysis of terminal (1->4)-linked alpha-D-glucose residues successively from non-reducing ends of the chains with release of beta-D-glucose. 3.2.1.3 -
-