› 2bv9

X-ray diffraction
1.5Å resolution

HOW FAMILY 26 GLYCOSIDE HYDROLASES ORCHESTRATE CATALYSIS ON DIFFERENT POLYSACCHARIDES. STRUCTURE AND ACTIVITY OF A CLOSTRIDIUM THERMOCELLUM LICHENASE, CtLIC26A

Released:
DOI: 10.2210/pdb2bv9/pdb
PDB entry 2bv9 coloured by chain, front view.
PDB entry 2bv9 coloured by chain, side view.
PDB entry 2bv9 coloured by chain, top view.
Source organism: Acetivibrio thermocellus
Primary publication:
How family 26 glycoside hydrolases orchestrate catalysis on different polysaccharides: structure and activity of a Clostridium thermocellum lichenase, CtLic26A.
Taylor EJ, Goyal A, Guerreiro CI, Prates JA, Money VA, Ferry N, Morland C, Planas A, Macdonald JA, Stick RV, Gilbert HJ, Fontes CM, Davies GJ
J Biol Chem 280 32761-7 (2005)
PMID: 15987675

Function and Biology Details

Reaction catalysed: 
Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-147658 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Endoglucanase H Chain: A
Molecule details ›
Chain: A
Length: 290 amino acids
Theoretical weight: 33.19 KDa
Source organism: Acetivibrio thermocellus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P16218 (Residues: 26-304; Coverage: 30%)
Gene names: Cthe_1472, celH
Sequence domains: Glycosyl hydrolase family 26
Structure domains: Glycosidases

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P212121
Unit cell:
a: 49.828Å b: 63.646Å c: 100.021Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.132 0.131 0.157
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

30 citation in other articles

The Cellvibrio japonicus mannanase CjMan26C displays a unique exo-mode of action that is conferred by subtle changes to the distal region of the active site.
Cartmell et al. (2008)
29 more

2 mentions without citation

The BioFragment Database (BFDb): An open-data platform for computational chemistry analysis of noncovalent interactions.
Burns et al. (2017)
1 more