› 2cit

X-ray diffraction
1.4Å resolution

Structure of the covalent intermediate of a family 26 lichenase

Released:
DOI: 10.2210/pdb2cit/pdb
PDB entry 2cit coloured by chain, front view.
PDB entry 2cit coloured by chain, side view.
PDB entry 2cit coloured by chain, top view.
Source organism: Acetivibrio thermocellus
Primary publication:
Substrate distortion by a lichenase highlights the different conformational itineraries harnessed by related glycoside hydrolases.
Money VA, Smith NL, Scaffidi A, Stick RV, Gilbert HJ, Davies GJ
Angew Chem Int Ed Engl 45 5136-40 (2006)
PMID: 16823793

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
Macromolecules (2 distinct):
Endoglucanase H Chain: A
Molecule details ›
Chain: A
Length: 282 amino acids
Theoretical weight: 32.06 KDa
Source organism: Acetivibrio thermocellus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P16218 (Residues: 25-304; Coverage: 30%)
Gene names: Cthe_1472, celH
Sequence domains: Glycosyl hydrolase family 26
Structure domains: Glycosidases

Ligands and Environments

Carbohydrate polymer : NEW Components: G2F, BGC
Carbohydrate polymer
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P212121
Unit cell:
a: 49.047Å b: 62.83Å c: 78.057Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.152 0.151 0.179
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Mechanistic insights into glycosidase chemistry.
Vocadlo et al. (2008)
11 other articles