› 1ouw

X-ray diffraction
1.37Å resolution

Crystal structure of Calystegia sepium agglutinin

Released:
DOI: 10.2210/pdb1ouw/pdb
PDB entry 1ouw coloured by chain, front view.
PDB entry 1ouw coloured by chain, side view.
PDB entry 1ouw coloured by chain, top view.
Source organism: Calystegia sepium
Primary publication:
The crystal structure of the Calystegia sepium agglutinin reveals a novel quaternary arrangement of lectin subunits with a beta-prism fold.
Bourne Y, Roig-Zamboni V, Barre A, Peumans WJ, Astoul CH, Van Damme EJ, Rougé P
J Biol Chem 279 527-33 (2004)
PMID: 14561768

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-161069 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Jacalin-related lectin Calsepa Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 152 amino acids
Theoretical weight: 15.99 KDa
Source organism: Calystegia sepium
UniProt:
  • Canonical: P93114 (Residues: 2-153; Coverage: 99%)
Sequence domains: Jacalin-like lectin domain
Structure domains: Jacalin-like lectin domain

Ligands and Environments

3 bound ligands:
Ligand EDO 9 x EDO
Ligand IMD 4 x IMD
Ligand MLT 2 x MLT
1 modified residue:
Ligand AYA 4 x AYA

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-3
Spacegroup: P1
Unit cell:
a: 30.562Å b: 51.792Å c: 79.78Å
α: 104.99° β: 94.36° γ: 94.85°
R-values:
R R work R free
0.153 0.153 0.18

Quick links

Citations

4 review citations

Role of receptors in Bacillus thuringiensis crystal toxin activity.
Pigott et al. (2007)
3 more

5 mentions without citation

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