› 1fny

X-ray diffraction
1.81Å resolution

LEGUME LECTIN OF THE BARK OF ROBINIA PSEUDOACACIA.

Released:
DOI: 10.2210/pdb1fny/pdb
PDB entry 1fny coloured by chain, front view.
PDB entry 1fny coloured by chain, side view.
PDB entry 1fny coloured by chain, top view.
Source organism: Robinia pseudoacacia
Primary publication:
Structure of a legume lectin from the bark of Robinia pseudoacacia and its complex with N-acetylgalactosamine.
Rabijns A, Verboven C, Rougé P, Barre A, Van Damme EJ, Peumans WJ, De Ranter CJ
Proteins 44 470-8 (2001)
PMID: 11484224

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-174942 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bark agglutinin I polypeptide A Chain: A
Molecule details ›
Chain: A
Length: 237 amino acids
Theoretical weight: 25.61 KDa
Source organism: Robinia pseudoacacia
UniProt:
  • Canonical: Q41159 (Residues: 32-268; Coverage: 93%)
Sequence domains: Legume lectin domain
Structure domains: Jelly Rolls

Ligands and Environments

1 bound ligand:
Ligand CA 1 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X11
Spacegroup: I222
Unit cell:
a: 64.078Å b: 75.854Å c: 118.084Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.191 0.189 0.211

Quick links

Citations

2 review citations

Lectins as bioactive plant proteins: a potential in cancer treatment.
De Mejía et al. (2005)
1 more

6 mentions without citation

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