› 2d7f

X-ray diffraction
2.31Å resolution

Crystal structure of A lectin from canavalia gladiata seeds complexed with alpha-methyl-mannoside and alpha-aminobutyric acid

Released:
DOI: 10.2210/pdb2d7f/pdb
PDB entry 2d7f coloured by chain, front view.
PDB entry 2d7f coloured by chain, side view.
PDB entry 2d7f coloured by chain, top view.
Source organism: Canavalia gladiata
Primary publication:
Structure of a lectin from Canavalia gladiata seeds: new structural insights for old molecules.
Delatorre P, Rocha BA, Souza EP, Oliveira TM, Bezerra GA, Moreno FB, Freitas BT, Santi-Gadelha T, Sampaio AH, Azevedo WF, Cavada BS
BMC Struct Biol 7 52 (2007)
PMID: 17683532

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-147131 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Concanavalin-A, 2nd part Chains: A, F, L, S
Molecule details ›
Chains: A, F, L, S
Length: 237 amino acids
Theoretical weight: 25.56 KDa
Source organism: Canavalia gladiata
UniProt:
  • Canonical: P14894 (Residues: 28-148; Coverage: 46%)
Sequence domains: Legume lectin domain
Structure domains: Jelly Rolls

Ligands and Environments

4 bound ligands:
Ligand MMA 4 x MMA
Ligand MN 4 x MN
Ligand CA 4 x CA
Ligand DBB 4 x DBB
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: LNLS BEAMLINE D03B-MX1
Spacegroup: C2221
Unit cell:
a: 100.915Å b: 115.754Å c: 241.626Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.182 0.18 0.227

Quick links

Citations

3 review citations

An overview of lectins purification strategies.
Nascimento et al. (2012)
2 more

3 mentions without citation

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