PDBe 1len

X-ray diffraction
1.8Å resolution

REFINEMENT OF TWO CRYSTAL FORMS OF LENTIL LECTIN AT 1.8 ANGSTROMS RESOLUTION

Released:

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Lectin beta chain Chains: A, C
Molecule details ›
Chains: A, C
Length: 181 amino acids
Theoretical weight: 19.91 KDa
Source organism: Lens culinaris
Expression system: Not provided
UniProt:
  • Canonical: P02870 (Residues: 31-211; Coverage: 74%)
Structure domains: Jelly Rolls
Lectin alpha chain Chains: B, D
Molecule details ›
Chains: B, D
Length: 52 amino acids
Theoretical weight: 5.71 KDa
Source organism: Lens culinaris
Expression system: Not provided
UniProt:
  • Canonical: P02870 (Residues: 218-269; Coverage: 21%)

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 58.49Å b: 56.37Å c: 82.73Å
α: 90° β: 104.4° γ: 90°
R-values:
R R work R free
0.175 not available not available
Expression system: Not provided