› 2bv4

X-ray diffraction
1Å resolution

1.0A Structure of Chromobacterium Violaceum Lectin in Complex with alpha-methyl-mannoside

Released:
DOI: 10.2210/pdb2bv4/pdb
PDB entry 2bv4 coloured by chain, front view.
PDB entry 2bv4 coloured by chain, side view.
PDB entry 2bv4 coloured by chain, top view.
Source organism: Chromobacterium violaceum
Primary publication:
Unusual entropy-driven affinity of Chromobacterium violaceum lectin CV-IIL toward fucose and mannose.
Pokorná M, Cioci G, Perret S, Rebuffet E, Kostlánová N, Adam J, Gilboa-Garber N, Mitchell EP, Imberty A, Wimmerová M
Biochemistry 45 7501-10 (2006)
PMID: 16768446

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-181846 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Calcium-mediated lectin domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 113 amino acids
Theoretical weight: 11.85 KDa
Source organism: Chromobacterium violaceum
Expression system: Escherichia coli
UniProt:
  • Canonical: Q7NX84 (Residues: 2-114; Coverage: 99%)
Gene name: CV_1744
Sequence domains: Fucose-binding lectin II (PA-IIL)
Structure domains: Calcium-mediated lectin

Ligands and Environments

2 bound ligands:
Ligand CA 4 x CA
Ligand MMA 2 x MMA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P21212
Unit cell:
a: 50.685Å b: 89.504Å c: 46.484Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.107 0.107 0.123
Expression system: Escherichia coli

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Citations

4 review citations

Biofilm Matrix Proteins.
Fong et al. (2015)
3 more

3 mentions without citation

Burkholderia cenocepacia BC2L-C is a super lectin with dual specificity and proinflammatory activity.
Sulák et al. (2011)
2 more