› 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 4l8q coloured by chain and viewed from the front.
PDB 4l8q coloured by chain and viewed from the side.
PDB 4l8q coloured by chain and viewed from the top.
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)
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

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Citations

1 review citation

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