› 2y6h

X-ray diffraction
1.08Å resolution

X-2 L110F CBM4-2 Carbohydrate Binding Module from a Thermostable Rhodothermus marinus Xylanase

Released:
DOI: 10.2210/pdb2y6h/pdb
PDB entry 2y6h coloured by chain, front view.
PDB entry 2y6h coloured by chain, side view.
PDB entry 2y6h coloured by chain, top view.
Source organism: Rhodothermus marinus
Primary publication:
Structural basis for carbohydrate-binding specificity--a comparative assessment of two engineered carbohydrate-binding modules.
von Schantz L, Håkansson M, Logan DT, Walse B, Osterlin J, Nordberg-Karlsson E, Ohlin M
Glycobiology 22 948-61 (2012)
PMID: 22434778

Function and Biology Details

Reaction catalysed: 
Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-182140 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
GH10 domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 167 amino acids
Theoretical weight: 17.94 KDa
Source organism: Rhodothermus marinus
Expression system: Escherichia coli K-12
UniProt:
  • Canonical: Q7WTN6 (Residues: 212-376; Coverage: 17%)
Sequence domains: Carbohydrate binding domain
Structure domains: Galactose-binding domain-like

Ligands and Environments

1 bound ligand:
Ligand CA 2 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX II BEAMLINE I911-2
Spacegroup: P212121
Unit cell:
a: 47.51Å b: 50.35Å c: 62.74Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.137 not available 0.17
Expression system: Escherichia coli K-12

Quick links

Citations

4 review citations

Advances in molecular engineering of carbohydrate-binding modules.
Armenta et al. (2017)
3 more

1 mention without citation

Exploring Structural Diversity among Adhesion Devices Encoded by Lactococcal P335 Phages with AlphaFold2.
Goulet et al. (2022)