› 5tg3

X-ray diffraction
1.76Å 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-110960 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lectin Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 237 amino acids
Theoretical weight: 25.59 KDa
Source organism: Macropsychanthus comosus
UniProt:
  • Canonical: C0HK81 (Residues: 1-237; Coverage: 100%)
Sequence domains: Legume lectin domain
Structure domains: Jelly Rolls

Ligands and Environments

3 bound ligands:
Ligand CA 4 x CA
Ligand MN 4 x MN
Ligand XMM 4 x XMM
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: LNLS BEAMLINE W01B-MX2
Spacegroup: P212121
Unit cell:
a: 72.46Å b: 85.18Å c: 174.58Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.218 0.217 0.249

Quick links

Citations

4 citation in other articles

Contribution of the carbohydrate-binding ability of Vatairea guianensis lectin to induce edematogenic activity.
Marques et al. (2017)
3 more

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