Structure analysis

Crystal structure of BclA lectin from burkholderia cenocepacia in complex with alpha-methyl-mannoside at 1.7 Angstrom resolution

X-ray diffraction
1.7Å resolution
Assembly composition:
homo dimer (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: homo dimer
Accessible surface area: 10700 Å2
Buried surface area: 4700 Å2
Dissociation area: 1,600 Å2
Dissociation energy (ΔGdiss): 11 kcal/mol
Dissociation entropy (TΔSdiss): 12 kcal/mol
Interface energy (ΔGint): -80 kcal/mol
Symmetry number: 2
Assembly 2
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Multimeric state: homo dimer

Binding statistics and energies are not available for this assembly
Assembly 3
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Multimeric state: homo dimer

Binding statistics and energies are not available for this assembly

Macromolecules

Chains: A, B, C, D, E
Length: 129 amino acids
Theoretical weight: 13.91 KDa
Source organism: Burkholderia cenocepacia J2315
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: B4EH87 (Residues: 1-129; Coverage: 100%)
Gene name: BCAM0186
Pfam: Fucose-binding lectin II (PA-IIL)
InterPro:
CATH: Calcium-mediated lectin

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