› 6a3h

X-ray diffraction
1.68Å resolution

2-DEOXY-2-FLURO-B-D-CELLOTRIOSYL/ENZYME INTERMEDIATE COMPLEX OF THE ENDOGLUCANASE CEL5A FROM BACILLUS AGARADHEARANS AT 1.6 ANGSTROM RESOLUTION

Released:
DOI: 10.2210/pdb6a3h/pdb
PDB entry 6a3h coloured by chain, front view.
PDB entry 6a3h coloured by chain, side view.
PDB entry 6a3h coloured by chain, top view.
Source organism: Salipaludibacillus agaradhaerens
Primary publication:
Snapshots along an enzymatic reaction coordinate: analysis of a retaining beta-glycoside hydrolase.
Davies GJ, Mackenzie L, Varrot A, Dauter M, Brzozowski AM, Schülein M, Withers SG
Biochemistry 37 11707-13 (1998)
PMID: 9718293

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-131438 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Endoglucanase 5A Chain: A
Molecule details ›
Chain: A
Length: 303 amino acids
Theoretical weight: 34 KDa
Source organism: Salipaludibacillus agaradhaerens
Expression system: Bacillus subtilis
UniProt:
  • Canonical: O85465 (Residues: 27-329; Coverage: 81%)
Gene name: cel5A
Sequence domains: Cellulase (glycosyl hydrolase family 5)
Structure domains: Glycosidases

Ligands and Environments

Carbohydrate polymer : NEW Components: G2F, BGC
Carbohydrate polymer
1 bound ligand:
Ligand GOL 8 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P212121
Unit cell:
a: 55.28Å b: 69.7Å c: 76.94Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.15 0.15 0.185
Expression system: Bacillus subtilis

Quick links

Citations

17 review citations

Glycosidase mechanisms.
Rye et al. (2000)
16 more

1 mention without citation

X-ray crystal structure of rabbit N-acetylglucosaminyltransferase I: catalytic mechanism and a new protein superfamily.
Unligil et al. (2000)