PDBe 3k8m

X-ray diffraction
2.5Å resolution

Crystal structure of SusG with acarbose

Released:

Function and Biology Details

Reaction catalysed:
Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units. 
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha-amylase SusG Chains: A, B
Molecule details ›
Chains: A, B
Length: 669 amino acids
Theoretical weight: 75.83 KDa
Source organism: Bacteroides thetaiotaomicron
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8A1G3 (Residues: 24-692; Coverage: 100%)
Gene names: BT_3698, susG
Sequence domains: Alpha amylase, catalytic domain
Structure domains:

Ligands and Environments


1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P41
Unit cell:
a: 127.709Å b: 127.709Å c: 127.987Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.201 0.201 0.247
Expression system: Escherichia coli