› 2f6d

X-ray diffraction
1.6Å resolution

Structure of the complex of a glucoamylase from Saccharomycopsis fibuligera with acarbose

Released:
DOI: 10.2210/pdb2f6d/pdb
PDB entry 2f6d coloured by chain, front view.
PDB entry 2f6d coloured by chain, side view.
PDB entry 2f6d 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
Macromolecules (2 distinct):
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

Carbohydrate polymer : NEW Components: GLC, AC1
Ligand GLC 4 x GLC
Ligand AC1 2 x AC1
2 bound ligands:
Ligand PO4 1 x PO4
Ligand NA 2 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X11
Spacegroup: P212121
Unit cell:
a: 56.58Å b: 85.35Å c: 97.51Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.12 0.118 0.16
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

Using Carbohydrate Interaction Assays to Reveal Novel Binding Sites in Carbohydrate Active Enzymes.
Cockburn et al. (2016)