› 3azz

X-ray diffraction
1.81Å resolution

Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 in complex with gluconolactone

Released:
DOI: 10.2210/pdb3azz/pdb
PDB entry 3azz coloured by chain, front view.
PDB entry 3azz coloured by chain, side view.
PDB entry 3azz coloured by chain, top view.
Source organism: Thermotoga maritima MSB8
Primary publication:
Crystal structures of the laminarinase catalytic domain from Thermotoga maritima MSB8 in complex with inhibitors: essential residues for β-1,3- and β-1,4-glucan selection.
Jeng WY, Wang NC, Lin CT, Shyur LF, Wang AH
J Biol Chem 286 45030-40 (2011)
PMID: 22065588

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-578100 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
GH16 domain-containing protein Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 272 amino acids
Theoretical weight: 31.24 KDa
Source organism: Thermotoga maritima MSB8
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9WXN1 (Residues: 204-466; Coverage: 41%)
Gene name: TM_0024
Sequence domains: Glycosyl hydrolases family 16
Structure domains: Jelly Rolls

Ligands and Environments

3 bound ligands:
Ligand LGC 3 x LGC
Ligand CA 4 x CA
Ligand SO4 8 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSRRC BEAMLINE BL13B1
Spacegroup: P212121
Unit cell:
a: 106.99Å b: 120.232Å c: 120.995Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.171 0.17 0.2
Expression system: Escherichia coli

Quick links

Citations

18 citation in other articles

The Recognition of Identical Ligands by Unrelated Proteins.
Barelier et al. (2015)
17 more

2 mentions without citation

Crystal structures of the laminarinase catalytic domain from Thermotoga maritima MSB8 in complex with inhibitors: essential residues for β-1,3- and β-1,4-glucan selection.
Jeng et al. (2011)
1 more