› 4b1m

X-ray diffraction
1.1Å resolution

CARBOHYDRATE BINDING MODULE CBM66 FROM BACILLUS SUBTILIS

Released:
DOI: 10.2210/pdb4b1m/pdb
PDB entry 4b1m coloured by chain, front view.
PDB entry 4b1m coloured by chain, side view.
PDB entry 4b1m coloured by chain, top view.
Source organism: Bacillus subtilis
Primary publication:
How nature can exploit nonspecific catalytic and carbohydrate binding modules to create enzymatic specificity.
Cuskin F, Flint JE, Gloster TM, Morland C, Baslé A, Henrissat B, Coutinho PM, Strazzulli A, Solovyova AS, Davies GJ, Gilbert HJ
Proc Natl Acad Sci U S A 109 20889-94 (2012)
PMID: 23213210

Function and Biology Details

Reaction catalysed: 
Hydrolysis of terminal, non-reducing (2->1)- and (2->6)-linked beta-D-fructofuranose residues in fructans
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-138730 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Levanase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 185 amino acids
Theoretical weight: 20.64 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli
UniProt:
  • Canonical: P05656 (Residues: 515-677; Coverage: 25%)
Gene names: BSU27030, sacC
Sequence domains: 3-keto-disaccharide hydrolase
Structure domains: Exo-inulinase; domain 1

Ligands and Environments

Carbohydrate polymer : NEW Components: FRU
Carbohydrate polymer
2 bound ligands:
Ligand NA 4 x NA
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I24
Spacegroup: P21
Unit cell:
a: 66.897Å b: 36.909Å c: 87.355Å
α: 90° β: 90.61° γ: 90°
R-values:
R R work R free
0.158 0.156 0.181
Expression system: Escherichia coli

Quick links

Citations

7 review citations

Advances in understanding the molecular basis of plant cell wall polysaccharide recognition by carbohydrate-binding modules.
Gilbert et al. (2013)
6 more

1 mention without citation

How nature can exploit nonspecific catalytic and carbohydrate binding modules to create enzymatic specificity.
Cuskin et al. (2012)