PDBe 2ltn

X-ray diffraction
1.7Å resolution

DESIGN, EXPRESSION, AND CRYSTALLIZATION OF RECOMBINANT LECTIN FROM THE GARDEN PEA (PISUM SATIVUM)

Released:

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
hetero tetramer
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Lectin alpha chain Chains: B, D
Molecule details ›
Chains: B, D
Length: 52 amino acids
Theoretical weight: 5.6 KDa
Source organism: Pisum sativum
Expression system: Not provided
UniProt:
  • Canonical: P02867 (Residues: 218-269; Coverage: 21%)
Gene names: LECA, PSL1
Lectin beta chain Chains: A, C
Molecule details ›
Chains: A, C
Length: 181 amino acids
Theoretical weight: 20 KDa
Source organism: Pisum sativum
Expression system: Escherichia coli
UniProt:
  • Canonical: P02867 (Residues: 31-211; Coverage: 74%)
Gene names: LECA, PSL1
Structure domains: Jelly Rolls

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 50.73Å b: 61.16Å c: 136.59Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.177 not available not available
Expression systems:
  • Not provided
  • Escherichia coli