3k8l

X-ray diffraction
2.3Å resolution

Crystal structure of SusG-D498N mutant with maltoheptaose

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)
Assembly name:
PDBe Complex ID:
PDB-CPX-183614 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (4 distinct):
Alpha-amylase SusG Chains: A, B
Molecule details ›
Chains: A, B
Length: 669 amino acids
Theoretical weight: 75.31 KDa
Source organism: Bacteroides thetaiotaomicron
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8A1G3 (Residues: 24-692; Coverage: 100%)
Gene names: BT_3698, susG
Sequence domains:
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: BGC, GLC
Carbohydrate polymer : NEW Components: GLC
Carbohydrate polymer : NEW Components: GLC
2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P41
Unit cell:
a: 128.041Å b: 128.041Å c: 130.483Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.184 0.184 0.216
Expression system: Escherichia coli