› 2vmi

X-ray diffraction
1.7Å resolution

The structure of seleno-methionine labelled CBM51 from Clostridium perfringens GH95

Released:
DOI: 10.2210/pdb2vmi/pdb
PDB entry 2vmi coloured by chain, front view.
PDB entry 2vmi coloured by chain, side view.
PDB entry 2vmi coloured by chain, top view.
Source organism: Clostridium perfringens
Primary publication:
Divergent modes of glycan recognition by a new family of carbohydrate-binding modules.
Gregg KJ, Finn R, Abbott DW, Boraston AB
J Biol Chem 283 12604-13 (2008)
PMID: 18292090

Function and Biology Details

Biochemical function:
  • not assigned
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-101668 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glycosyl hydrolase family 98 putative carbohydrate-binding module domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 151 amino acids
Theoretical weight: 16.39 KDa
Source organism: Clostridium perfringens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: A0A0H2YQB3 (Residues: 900-1050; Coverage: 10%)
Gene name: CPF_2129
Sequence domains: NPCBM/NEW2 domain
Structure domains: NPCBM/NEW2 domain

Ligands and Environments

1 bound ligand:
Ligand CA 1 x CA
1 modified residue:
Ligand MSE 2 x MSE

Experiments and Validation Details

Entry percentile scores
Spacegroup: P65
Unit cell:
a: 76.721Å b: 76.721Å c: 51.771Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.151 0.15 0.178
Expression system: Escherichia coli BL21

Quick links

Citations

9 review citations

Carbohydrate-binding domains: multiplicity of biological roles.
Guillén et al. (2010)
8 more

1 mention without citation

Divergent modes of glycan recognition by a new family of carbohydrate-binding modules.
Gregg et al. (2008)