2wq4

X-ray diffraction
1.42Å resolution

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

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
PA-IIL domain-containing protein Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 156 amino acids
Theoretical weight: 15.96 KDa
Source organism: Burkholderia cenocepacia J2315
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: B4EH86 (Residues: 1-156; Coverage: 57%)
Gene name: BCAM0185
Structure domains: Jelly Rolls

Ligands and Environments

2 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P212121
Unit cell:
a: 43.1Å b: 76.73Å c: 103.26Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.133 0.131 0.166
Expression system: Escherichia coli BL21(DE3)