› 2ef6

X-ray diffraction
2.1Å resolution

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-147131 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Concanavalin-A, 2nd part Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 237 amino acids
Theoretical weight: 25.56 KDa
Source organism: Canavalia gladiata
UniProt:
  • Canonical: P14894 (Residues: 28-148; Coverage: 46%)
Sequence domains: Legume lectin domain
Structure domains: Jelly Rolls

Ligands and Environments

Carbohydrate polymer : NEW Components: MMA, MAN
Carbohydrate polymer
2 bound ligands:
Ligand CA 4 x CA
Ligand MN 4 x MN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: LNLS BEAMLINE D03B-MX1
Spacegroup: P32
Unit cell:
a: 69.391Å b: 69.391Å c: 161.298Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.192 0.189 0.245

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

1 mention without citation

Overview of the Structure⁻Function Relationships of Mannose-Specific Lectins from Plants, Algae and Fungi.
Barre et al. (2019)