› 3wcr

X-ray diffraction
2.45Å resolution

Crystal structure of plant lectin (ligand-free form)

Released:
DOI: 10.2210/pdb3wcr/pdb
PDB entry 3wcr coloured by chain, front view.
PDB entry 3wcr coloured by chain, side view.
PDB entry 3wcr coloured by chain, top view.
Source organism: Phaseolus vulgaris
Primary publication:
Phytohemagglutinin from Phaseolus vulgaris (PHA-E) displays a novel glycan recognition mode using a common legume lectin fold.
Nagae M, Soga K, Morita-Matsumoto K, Hanashima S, Ikeda A, Yamamoto K, Yamaguchi Y
Glycobiology 24 368-78 (2014)
PMID: 24436051

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-529024 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Erythroagglutinating phytohemagglutinin Chains: A, B
Molecule details ›
Chains: A, B
Length: 254 amino acids
Theoretical weight: 27.62 KDa
Source organism: Phaseolus vulgaris
UniProt:
  • Canonical: P05088 (Residues: 22-275; Coverage: 100%)
Gene name: DLEC1
Sequence domains: Legume lectin domain
Structure domains: Jelly Rolls

Ligands and Environments

2 bound ligands:
Ligand NAG 2 x NAG
Ligand BR 19 x BR
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-17A
Spacegroup: P41212
Unit cell:
a: 68.856Å b: 68.856Å c: 242.539Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.215 0.213 0.257

Quick links

Citations

11 review citations

Legume Lectins: Proteins with Diverse Applications.
Lagarda-Diaz et al. (2017)
10 more

1 mention without citation

Overview of the Structure⁻Function Relationships of Mannose-Specific Lectins from Plants, Algae and Fungi.
Barre et al. (2019)