› 1jn2

X-ray diffraction
1.9Å resolution

Crystal Structure of meso-tetrasulphonatophenyl porphyrin complexed with Concanavalin A

Released:
DOI: 10.2210/pdb1jn2/pdb
PDB entry 1jn2 coloured by chain, front view.
PDB entry 1jn2 coloured by chain, side view.
PDB entry 1jn2 coloured by chain, top view.
Source organism: Canavalia ensiformis
Primary publication:
Functional equality in the absence of structural similarity: an added dimension to molecular mimicry.
Goel M, Jain D, Kaur KJ, Kenoth R, Maiya BG, Swamy MJ, Salunke DM
J Biol Chem 276 39277-81 (2001)
PMID: 11504727

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-136268 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Concanavalin-A, 2nd part Chain: P
Molecule details ›
Chain: P
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

3 bound ligands:
Ligand CA 1 x CA
Ligand MN 1 x MN
Ligand SFP 1 x SFP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: F222
Unit cell:
a: 106Å b: 117.3Å c: 126Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.195 0.195 0.232

Quick links

Citations

3 review citations

Beyond carbohydrate binding: new directions in plant lectin research.
Komath et al. (2006)
2 more

1 mention without citation

Protein-macrocycle polymorphism: crystal form IV of the Ralstonia solanacearum lectin-sulfonato-calix[8]arene complex.
Mockler et al. (2023)