› 1w8u

X-ray diffraction
1.3Å resolution

CBM29-2 mutant D83A complexed with mannohexaose: Probing the Mechanism of Ligand Recognition by Family 29 Carbohydrate Binding Modules

Released:
DOI: 10.2210/pdb1w8u/pdb
PDB 1w8u coloured by chain and viewed from the front.
PDB 1w8u coloured by chain and viewed from the side.
PDB 1w8u coloured by chain and viewed from the top.
Source organism: Piromyces sp. 'equi'
Primary publication:
Probing the mechanism of ligand recognition in family 29 carbohydrate-binding modules.
Flint J, Bolam DN, Nurizzo D, Taylor EJ, Williamson MP, Walters C, Davies GJ, Gilbert HJ
J. Biol. Chem. 280 23718-26 (2005)
PMID: 15784618

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
CBM10 domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 149 amino acids
Theoretical weight: 16.62 KDa
Source organism: Piromyces sp. 'equi'
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9C171 (Residues: 334-478; Coverage: 32%)
Gene name: ncp1
Structure domains: Galactose-binding lectin

Ligands and Environments

Carbohydrate polymer : NEW Components: BMA
Carbohydrate polymer
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX9.6
Spacegroup: C2
Unit cell:
a: 51.15Å b: 42.636Å c: 60.182Å
α: 90° β: 93.71° γ: 90°
R-values:
R R work R free
0.162 0.161 0.175
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Carbohydrate-binding domains: multiplicity of biological roles.
Guillén et al. (2010)
18 other articles