› 2y64

X-ray diffraction
1.4Å resolution

Xylopentaose binding mutated (X-2 L110F) CBM4-2 Carbohydrate Binding Module from a Thermostable Rhodothermus marinus Xylanase

Released:
DOI: 10.2210/pdb2y64/pdb
PDB entry 2y64 coloured by chain, front view.
PDB entry 2y64 coloured by chain, side view.
PDB entry 2y64 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
Macromolecules (2 distinct):
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

Carbohydrate polymer : NEW Components: XYP
Carbohydrate polymer
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: 48.46Å b: 50.68Å c: 62.55Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.143 not available 0.2
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

Structural basis of the Cope rearrangement and cyclization in hapalindole biogenesis.
Newmister et al. (2018)