› 1lul

X-ray diffraction
3.3Å resolution

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-148652 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lectin DB58 Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 253 amino acids
Theoretical weight: 27.15 KDa
Source organism: Vigna unguiculata subsp. cylindrica
UniProt:
  • Canonical: P19588 (Residues: 23-275; Coverage: 100%)
Sequence domains: Legume lectin domain
Structure domains: Jelly Rolls

Ligands and Environments

2 bound ligands:
Ligand MN 6 x MN
Ligand CA 6 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX7.2
Spacegroup: P212121
Unit cell:
a: 101.39Å b: 130.95Å c: 138.23Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.226 0.226 0.266

Quick links

Citations

7 review citations

Lectins.
Vijayan et al. (1999)
6 more

3 mentions without citation

Research advances and prospects of legume lectins.
Katoch et al. (2021)
2 more