› 2cyf

X-ray diffraction
1.8Å resolution

The Crystal Structure of Canavalia Maritima Lectin (ConM) in Complex with Trehalose and Maltose

Released:
DOI: 10.2210/pdb2cyf/pdb
PDB entry 2cyf coloured by chain, front view.
PDB entry 2cyf coloured by chain, side view.
PDB entry 2cyf coloured by chain, top view.
Source organism: Canavalia rosea
Primary publication:
Crystal structure of a lectin from Canavalia maritima (ConM) in complex with trehalose and maltose reveals relevant mutation in ConA-like lectins.
Delatorre P, Rocha BA, Gadelha CA, Santi-Gadelha T, Cajazeiras JB, Souza EP, Nascimento KS, Freire VN, Sampaio AH, Azevedo WF, Cavada BS
J Struct Biol 154 280-6 (2006)
PMID: 16677825

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-157353 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Concanavalin-Br Chains: A, C
Molecule details ›
Chains: A, C
Length: 237 amino acids
Theoretical weight: 25.49 KDa
Source organism: Canavalia rosea
UniProt:
  • Canonical: P55915 (Residues: 1-237; Coverage: 100%)
Sequence domains: Legume lectin domain
Structure domains: Jelly Rolls

Ligands and Environments

Carbohydrate polymer : NEW Components: GLC
Carbohydrate polymer
2 bound ligands:
Ligand CA 2 x CA
Ligand MN 2 x MN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: LNLS BEAMLINE D03B-MX1
Spacegroup: P21212
Unit cell:
a: 67.033Å b: 97.332Å c: 71.086Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.198 0.186 0.238

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Citations

1 review citation

The Updated Review on Plant Peptides and Their Applications in Human Health.
Mani et al. (2022)
10 other articles