› 4l8q

X-ray diffraction
2.3Å resolution

Crystal structure of Canavalia grandiflora seed lectin complexed with X-Man.

Released:
DOI: 10.2210/pdb4l8q/pdb
PDB entry 4l8q coloured by chain, front view.
PDB entry 4l8q coloured by chain, side view.
PDB entry 4l8q coloured by chain, top view.
Source organism: Canavalia grandiflora
Primary publication:
Vasorelaxant activity of Canavalia grandiflora seed lectin: A structural analysis.
Barroso-Neto IL, Simões RC, Rocha BA, Bezerra MJ, Pereira-Junior FN, Silva Osterne VJ, Nascimento KS, Nagano CS, Delatorre P, Pereira MG, Freitas Pires A, Sampaio AH, Assreuy AM, Cavada BS
Arch Biochem Biophys 543 31-9 (2014)
PMID: 24361256

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-100369 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lectin ConGF Chain: A
Molecule details ›
Chain: A
Length: 237 amino acids
Theoretical weight: 25.63 KDa
Source organism: Canavalia grandiflora
UniProt:
  • Canonical: A0A067XG71 (Residues: 1-237; Coverage: 100%)
Sequence domains: Legume lectin domain
Structure domains: Jelly Rolls

Ligands and Environments

6 bound ligands:
Ligand CA 1 x CA
Ligand MN 1 x MN
Ligand XMM 1 x XMM
Ligand SO4 1 x SO4
Ligand CD 2 x CD
Ligand GOL 3 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: LNLS BEAMLINE D03B-MX1
Spacegroup: I222
Unit cell:
a: 63.422Å b: 65.152Å c: 106.708Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.228 0.226 0.267

Quick links

Citations

2 review citations

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

3 mentions without citation

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