› 3ju9

X-ray diffraction
2.1Å resolution

Crystal structure of a lectin from Canavalia brasiliensis seed (ConBr) complexed with alpha-aminobutyric acid

Released:
DOI: 10.2210/pdb3ju9/pdb
PDB entry 3ju9 coloured by chain, front view.
PDB entry 3ju9 coloured by chain, side view.
PDB entry 3ju9 coloured by chain, top view.
Source organism: Canavalia brasiliensis
Primary publication:
Structural analysis of ConBr reveals molecular correlation between the carbohydrate recognition domain and endothelial NO synthase activation.
Bezerra EH, Rocha BA, Nagano CS, Bezerra Gde A, Moura TR, Bezerra MJ, Benevides RG, Sampaio AH, Assreuy AM, Delatorre P, Cavada BS
Biochem Biophys Res Commun 408 566-70 (2011)
PMID: 21530490

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-157353 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Concanavalin-Br Chain: A
Molecule details ›
Chain: A
Length: 237 amino acids
Theoretical weight: 25.59 KDa
Source organism: Canavalia brasiliensis
UniProt:
  • Canonical: P55915 (Residues: 1-237; Coverage: 100%)
Sequence domains: Legume lectin domain
Structure domains: Jelly Rolls

Ligands and Environments

5 bound ligands:
Ligand DBB 1 x DBB
Ligand GOL 1 x GOL
Ligand CA 1 x CA
Ligand MN 1 x MN
Ligand CL 2 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: LNLS BEAMLINE D03B-MX1
Spacegroup: I222
Unit cell:
a: 68.323Å b: 73.02Å c: 99.542Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.207 0.204 0.253

Quick links

Citations

2 review citations

ConA-Like Lectins: High Similarity Proteins as Models to Study Structure/Biological Activities Relationships.
Cavada et al. (2018)
1 more

5 mentions without citation

Research advances and prospects of legume lectins.
Katoch et al. (2021)
4 more