› 2xhj

X-ray diffraction
1.73Å resolution

Circular permutation provides an evolutionary link between two families of calcium-dependent carbohydrate binding modules. SeMet form of vCBM60.

Released:
DOI: 10.2210/pdb2xhj/pdb
PDB 2xhj coloured by chain and viewed from the front.
PDB 2xhj coloured by chain and viewed from the side.
PDB 2xhj coloured by chain and viewed from the top.
Source organism: Cellvibrio japonicus
Primary publication:
Circular permutation provides an evolutionary link between two families of calcium-dependent carbohydrate binding modules.
Montanier C, Flint JE, Bolam DN, Xie H, Liu Z, Rogowski A, Weiner DP, Ratnaparkhe S, Nurizzo D, Roberts SM, Turkenburg JP, Davies GJ, Gilbert HJ
J Biol Chem 285 31742-54 (2010)
PMID: 20659893

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
CALCIUM-DEPENDENT CARBOHYDRATE BINDING MODULE Chain: A
Molecule details ›
Chain: A
Length: 119 amino acids
Theoretical weight: 12.93 KDa
Source organism: Cellvibrio japonicus
Expression system: Escherichia coli
Structure domains: Lipoxygenase-1

Ligands and Environments

1 bound ligand:
Ligand CA 1 x CA
1 modified residue:
Ligand MSE 1 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P41212
Unit cell:
a: 45.805Å b: 45.805Å c: 102.439Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.13 0.126 0.217
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Carbohydrate Binding Modules: Diversity of Domain Architecture in Amylases and Cellulases From Filamentous Microorganisms.
Sidar et al. (2020)
3 more

1 mention without citation

Circular permutation provides an evolutionary link between two families of calcium-dependent carbohydrate binding modules.
Montanier et al. (2010)