› 1dq6

X-ray diffraction
1.9Å resolution

Manganese;Manganese concanavalin A at pH 7.0

Released:
DOI: 10.2210/pdb1dq6/pdb
PDB entry 1dq6 coloured by chain, front view.
PDB entry 1dq6 coloured by chain, side view.
PDB entry 1dq6 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:
  • 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-136271 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Concanavalin-A, 2nd part Chain: A
Molecule details ›
Chain: A
Length: 237 amino acids
Theoretical weight: 25.62 KDa
Source organism: Canavalia ensiformis
UniProt:
  • Canonical: P02866 (Residues: 28-148; Coverage: 46%)
Sequence domains: Legume lectin domain
Structure domains: Jelly Rolls

Ligands and Environments

1 bound ligand:
Ligand MN 2 x MN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ENRAF-NONIUS FR571
Spacegroup: I222
Unit cell:
a: 63.2Å b: 87.41Å c: 89.3Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.186 0.186 not available

Quick links

Citations

3 review citations

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

4 mentions without citation

Understanding protein structure from a percolation perspective.
Deb et al. (2009)
3 more