› 5f5q

X-ray diffraction
2.52Å resolution

Crystal structure of Canavalia virosa lectin in complex with alpha-methyl-mannoside

Released:
DOI: 10.2210/pdb5f5q/pdb
PDB entry 5f5q coloured by chain, front view.
PDB entry 5f5q coloured by chain, side view.
PDB entry 5f5q coloured by chain, top view.
Source organism: Canavalia cathartica
Primary publication:
Structural characterization of a lectin from Canavalia virosa seeds with inflammatory and cytotoxic activities.
Osterne VJS, Silva-Filho JC, Santiago MQ, Pinto-Junior VR, Almeida AC, Barreto AAGC, Wolin IAV, Nascimento APM, Amorim RMF, Rocha BAM, Delatorre P, Nagano CS, Leal RB, Assreuy AMS, Nascimento KS, Cavada BS
Int J Biol Macromol 94 271-282 (2017)
PMID: 27737777

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-110953 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Concanavalin V Chains: A, B
Molecule details ›
Chains: A, B
Length: 237 amino acids
Theoretical weight: 25.5 KDa
Source organism: Canavalia cathartica
UniProt:
  • Canonical: C0HJY1 (Residues: 1-237; Coverage: 100%)
Sequence domains: Legume lectin domain
Structure domains: Jelly Rolls

Ligands and Environments

3 bound ligands:
Ligand CA 2 x CA
Ligand MN 2 x MN
Ligand MMA 2 x MMA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: LNLS BEAMLINE W01B-MX2
Unit cell:
a: 60.25Å b: 81.74Å c: 86.93Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.188 0.184 0.251

Quick links

Citations

1 review citation

Plant lectins as potent Anti-coronaviruses, Anti-inflammatory, antinociceptive and antiulcer agents.
Konozy et al. (2022)
8 other articles

2 mentions without citation

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