› 1k42

Solution NMR

The Solution Structure of the CBM4-2 Carbohydrate Binding Module from a Thermostable Rhodothermus marinus Xylanase.

Released:
DOI: 10.2210/pdb1k42/pdb
PDB entry 1k42 coloured by chain, ensemble of 12 models, front view.
PDB entry 1k42 coloured by chain, ensemble of 12 models, side view.
PDB entry 1k42 coloured by chain, ensemble of 12 models, top view.
Source organism: Rhodothermus marinus
Primary publication:
The solution structure of the CBM4-2 carbohydrate binding module from a thermostable Rhodothermus marinus xylanase.
Simpson PJ, Jamieson SJ, Abou-Hachem M, Karlsson EN, Gilbert HJ, Holst O, Williamson MP
Biochemistry 41 5712-9 (2002)
PMID: 11980475

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 domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-161266 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
GH10 domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 168 amino acids
Theoretical weight: 18.1 KDa
Source organism: Rhodothermus marinus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P96988 (Residues: 113-121, 122-151; Coverage: 10%)
Structure domains: Galactose-binding domain-like

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: hybrid distance geometry/simulated annealing using XPLOR
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

12 review citations

Current strategies for the use of affinity tags and tag removal for the purification of recombinant proteins.
Arnau et al. (2006)
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10 mentions without citation

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Venditto et al. (2016)
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