› 1dq0

X-ray diffraction
1.7Å resolution

Locked, metal-free concanavalin A, a minor species in solution

Released:
DOI: 10.2210/pdb1dq0/pdb
PDB entry 1dq0 coloured by chain, front view.
PDB entry 1dq0 coloured by chain, side view.
PDB entry 1dq0 coloured by chain, top view.
Source organism: Canavalia ensiformis
Primary publication:
The structural features of concanavalin A governing non-proline peptide isomerization.
Bouckaert J, Dewallef Y, Poortmans F, Wyns L, Loris R
J Biol Chem 275 19778-87 (2000)
PMID: 10748006

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-157353 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Concanavalin-Br Chain: A
Molecule details ›
Chain: A
Length: 237 amino acids
Theoretical weight: 25.62 KDa
Source organism: Canavalia ensiformis
UniProt:
  • Canonical: P55915 (Residues: 1-237; Coverage: 100%)
Sequence domains: Legume lectin domain
Structure domains: Jelly Rolls

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: I222
Unit cell:
a: 63.006Å b: 87.29Å c: 88.807Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.181 0.181 0.204

Quick links

Citations

3 review citations

Plant lectins: occurrence, biochemistry, functions and applications.
Rüdiger et al. (2001)
2 more

3 mentions without citation

Structural and functional diversity of the lectin repertoire in teleost fish: relevance to innate and adaptive immunity.
Vasta et al. (2011)
2 more