› 3n36

X-ray diffraction
2.3Å resolution

Erythrina corallodendron lectin mutant (Y106G) in complex with Galactose

Released:
DOI: 10.2210/pdb3n36/pdb
PDB entry 3n36 coloured by chain, front view.
PDB entry 3n36 coloured by chain, side view.
PDB entry 3n36 coloured by chain, top view.
Source organism: Erythrina corallodendron
Primary publication:
Modification of the sugar specificity of a plant lectin: structural studies on a point mutant of Erythrina corallodendron lectin.
Thamotharan S, Karthikeyan T, Kulkarni KA, Shetty KN, Surolia A, Vijayan M, Suguna K
Acta Crystallogr D Biol Crystallogr 67 218-27 (2011)
PMID: 21358053

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-147700 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lectin Chain: A
Molecule details ›
Chain: A
Length: 242 amino acids
Theoretical weight: 26.49 KDa
Source organism: Erythrina corallodendron
Expression system: Escherichia coli
UniProt:
  • Canonical: P16404 (Residues: 27-268; Coverage: 95%)
Sequence domains: Legume lectin domain
Structure domains: Jelly Rolls

Ligands and Environments

3 bound ligands:
Ligand MN 1 x MN
Ligand CA 1 x CA
Ligand GLA 1 x GLA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P3121
Unit cell:
a: 102.584Å b: 102.584Å c: 57.112Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.177 0.177 0.208
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Lectin engineering, a molecular evolutionary approach to expanding the lectin utilities.
Hu et al. (2015)
1 other article