› 2fba

X-ray diffraction
1.1Å resolution

Glucoamylase from Saccharomycopsis fibuligera at atomic resolution

Released:
DOI: 10.2210/pdb2fba/pdb
PDB entry 2fba coloured by chain, front view.
PDB entry 2fba coloured by chain, side view.
PDB entry 2fba coloured by chain, top view.
Source organism: Saccharomycopsis fibuligera
Primary publication:
Structure of the complex of a yeast glucoamylase with acarbose reveals the presence of a raw starch binding site on the catalytic domain.
Sevcík J, Hostinová E, Solovicová A, Gasperík J, Dauter Z, Wilson KS
FEBS J 273 2161-71 (2006)
PMID: 16649993

Function and Biology Details

Reaction catalysed: 
Hydrolysis of terminal (1->4)-linked alpha-D-glucose residues successively from non-reducing ends of the chains with release of beta-D-glucose
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139889 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glucoamylase GLU1 Chain: A
Molecule details ›
Chain: A
Length: 492 amino acids
Theoretical weight: 54.66 KDa
Source organism: Saccharomycopsis fibuligera
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P08017 (Residues: 28-519; Coverage: 100%)
Gene name: GLU1
Sequence domains: Glycosyl hydrolases family 15
Structure domains: Glycosyltransferase

Ligands and Environments

1 bound ligand:
Ligand TRS 1 x TRS
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE BW7B
Spacegroup: P212121
Unit cell:
a: 56.901Å b: 85.696Å c: 98.237Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.146 0.145 0.161
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

5 review citations

Occurrence and functional significance of secondary carbohydrate binding sites in glycoside hydrolases.
Cuyvers et al. (2012)
4 more

1 mention without citation

Structure of the catalytic domain of glucoamylase from Aspergillus niger.
Lee et al. (2011)