› 2w9x

X-ray diffraction
2Å resolution

The active site of a carbohydrate esterase displays divergent catalytic and non-catalytic binding functions

Released:
DOI: 10.2210/pdb2w9x/pdb
PDB entry 2w9x coloured by chain, front view.
PDB entry 2w9x coloured by chain, side view.
PDB entry 2w9x coloured by chain, top view.
Source organism: Cellvibrio japonicus
Primary publication:
The active site of a carbohydrate esterase displays divergent catalytic and noncatalytic binding functions.
Montanier C, Money VA, Pires VM, Flint JE, Pinheiro BA, Goyal A, Prates JA, Izumi A, Stålbrand H, Morland C, Cartmell A, Kolenova K, Topakas E, Dodson EJ, Bolam DN, Davies GJ, Fontes CM, Gilbert HJ
PLoS Biol 7 e71 (2009)
PMID: 19338387

Function and Biology Details

Reaction catalysed: 
Deacetylation of xylans and xylo-oligosaccharides
Biochemical function:
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-109889 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Acetylxylan esterase / glucomannan deacetylase Chains: A, B
Molecule details ›
Chains: A, B
Length: 366 amino acids
Theoretical weight: 40.91 KDa
Source organism: Cellvibrio japonicus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: B3PDE5 (Residues: 1-360; Coverage: 100%)
Gene names: CJA_3103, ce2C
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand GOL 7 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P43
Unit cell:
a: 75.274Å b: 75.274Å c: 141.62Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.193 0.191 0.231
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

8 review citations

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

2 mentions without citation

The SGNH hydrolase family: a template for carbohydrate diversity.
Anderson et al. (2022)
1 more