› 2c26

X-ray diffraction
2.1Å resolution

Structural basis for the promiscuous specificity of the carbohydrate- binding modules from the beta-sandwich super family

Released:
DOI: 10.2210/pdb2c26/pdb
Model geometry
Fit model/data
PDB entry 2c26 coloured by chain, front view.
PDB entry 2c26 coloured by chain, side view.
PDB entry 2c26 coloured by chain, top view.
Source organism: Acetivibrio thermocellus
Primary publication:
Xyloglucan is recognized by carbohydrate-binding modules that interact with beta-glucan chains.
Najmudin S, Guerreiro CI, Carvalho AL, Prates JA, Correia MA, Alves VD, Ferreira LM, Romão MJ, Gilbert HJ, Bolam DN, Fontes CM
J Biol Chem 281 8815-28 (2006)
PMID: 16314409

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-107039 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glycoside hydrolase family 9 Chain: A
Molecule details ›
Chain: A
Length: 260 amino acids
Theoretical weight: 28.64 KDa
Source organism: Acetivibrio thermocellus
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: A3DD30 (Residues: 1353-1601; Coverage: 16%)
Gene name: Cthe_0624
Sequence domains: PKD domain
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand CA 2 x CA
Ligand EDO 12 x EDO
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P43212
Unit cell:
a: 87.469Å b: 87.469Å c: 103.189Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.176 0.174 0.22
Expression system: Escherichia coli BL21

Quick links

Citations

8 review citations

Cellulosomes: highly efficient nanomachines designed to deconstruct plant cell wall complex carbohydrates.
Fontes et al. (2010)
7 more

5 mentions without citation

Re-evaluation of a bacterial antifreeze protein as an adhesin with ice-binding activity.
Guo et al. (2012)
4 more