X-ray diffraction
1.9Å resolution

Ensemble refinement of the E502A variant of sacteLam55A from Streptomyces sp. SirexAA-E in complex with laminaritetraose


Function and Biology Details

Reaction catalysed:
Successive hydrolysis of beta-D-glucose units from the non-reducing ends of (1->3)-beta-D-glucans, releasing alpha-glucose
Biological process:
Cellular component:
Sequence domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Exo-beta-1,3-glucanase Chain: A
Molecule details ›
Chain: A
Length: 549 amino acids
Theoretical weight: 58.88 KDa
Source organism: Streptomyces sp. SirexAA-E
Expression system: Escherichia coli BL21(DE3)
  • Canonical: G2NFJ9 (Residues: 57-605; Coverage: 98%)
Gene name: SACTE_4363

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-G
Spacegroup: P21
Unit cell:
a: 51.276Å b: 100.21Å c: 54.223Å
α: 90° β: 99.46° γ: 90°
R R work R free
0.115 0.113 0.151
Expression system: Escherichia coli BL21(DE3)