› 2xr4

X-ray diffraction
1.9Å resolution

C-terminal domain of BC2L-C Lectin from Burkholderia cenocepacia

Released:
DOI: 10.2210/pdb2xr4/pdb
PDB entry 2xr4 coloured by chain, front view.
PDB entry 2xr4 coloured by chain, side view.
PDB entry 2xr4 coloured by chain, top view.
Source organism: Burkholderia cenocepacia J2315
Primary publication:
Burkholderia cenocepacia BC2L-C is a super lectin with dual specificity and proinflammatory activity.
Sulák O, Cioci G, Lameignère E, Balloy V, Round A, Gutsche I, Malinovská L, Chignard M, Kosma P, Aubert DF, Marolda CL, Valvano MA, Wimmerová M, Imberty A
OpenAccess logo PLoS Pathog 7 e1002238 (2011)
PMID: 21909279

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-110044 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lectin Chains: A, B
Molecule details ›
Chains: A, B
Length: 116 amino acids
Theoretical weight: 12.58 KDa
Source organism: Burkholderia cenocepacia J2315
Expression system: Escherichia coli
UniProt:
  • Canonical: B4EH86 (Residues: 158-272; Coverage: 42%)
Gene name: BCAM0185
Sequence domains: Fucose-binding lectin II (PA-IIL)
Structure domains: Calcium-mediated lectin

Ligands and Environments

1 bound ligand:
Ligand SO4 2 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P65
Unit cell:
a: 100.814Å b: 100.814Å c: 47.313Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.158 0.156 0.199
Expression system: Escherichia coli

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Citations

5 review citations

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Geissner et al. (2014)
4 more

4 mentions without citation

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Mauracher et al. (2014)
3 more