› 2c3h

X-ray diffraction
2.24Å resolution

Structure of CBM26 from Bacillus halodurans amylase in complex with maltose

Released:
DOI: 10.2210/pdb2c3h/pdb
PDB entry 2c3h coloured by chain, front view.
PDB entry 2c3h coloured by chain, side view.
PDB entry 2c3h coloured by chain, top view.
Source organism: Alkalihalobacillus halodurans C-125
Primary publication:
A structural and functional analysis of alpha-glucan recognition by family 25 and 26 carbohydrate-binding modules reveals a conserved mode of starch recognition.
Boraston AB, Healey M, Klassen J, Ficko-Blean E, Lammerts van Bueren A, Law V
J Biol Chem 281 587-98 (2006)
PMID: 16230347

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-191868 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Alpha-amylase G-6 Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 98 amino acids
Theoretical weight: 11.46 KDa
Source organism: Alkalihalobacillus halodurans C-125
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9KFR4 (Residues: 769-863; Coverage: 10%)
Gene name: BH0413
Sequence domains: Starch-binding module 26
Structure domains: Immunoglobulins

Ligands and Environments

Carbohydrate polymer : NEW Components: GLC
Carbohydrate polymer
2 bound ligands:
Ligand SO4 9 x SO4
Ligand GLC 1 x GLC
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P3221
Unit cell:
a: 108.204Å b: 108.204Å c: 180.493Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.207 0.203 0.279
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

10 review citations

α-Amylase: an enzyme specificity found in various families of glycoside hydrolases.
Janeček et al. (2014)
9 more

1 mention without citation

Novel carbohydrate binding modules in the surface anchored α-amylase of Eubacterium rectale provide a molecular rationale for the range of starches used by this organism in the human gut.
Cockburn et al. (2018)