X-ray diffraction
1.8Å resolution

Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8


Function and Biology Details

Reaction catalysed:
Hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
GH16 domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 272 amino acids
Theoretical weight: 31.24 KDa
Source organism: Thermotoga maritima MSB8
Expression system: Escherichia coli
  • Canonical: Q9WXN1 (Residues: 204-466; Coverage: 41%)
Gene name: TM_0024
Sequence domains: Glycosyl hydrolases family 16
Structure domains: Jelly Rolls

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSRRC BEAMLINE BL13B1
Spacegroup: C2
Unit cell:
a: 100.567Å b: 56.152Å c: 126.431Å
α: 90° β: 105.26° γ: 90°
R R work R free
0.201 0.198 0.248
Expression system: Escherichia coli