› 1vln

X-ray diffraction
2.4Å resolution

A TRICLINIC CRYSTAL FORM OF THE LECTIN CONCANAVALIN A

Released:
DOI: 10.2210/pdb1vln/pdb
PDB entry 1vln coloured by chain, front view.
PDB entry 1vln coloured by chain, side view.
PDB entry 1vln coloured by chain, top view.
Source organism: Canavalia ensiformis
Primary publication:
A Triclinic Crystal Form of the Lectin Concanavalin A
Kanellopoulos PN, Tucker PA, Pavlou K, Agianian B, Hamodrakas SJ
J Struct Biol 117 16-23 (1996)
PMID: 8812975

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-140420 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lectin alpha chain Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 237 amino acids
Theoretical weight: 25.62 KDa
Source organism: Canavalia ensiformis
UniProt:
  • Canonical: P08902 (Residues: 1-237; Coverage: 100%)
Sequence domains: Legume lectin domain
Structure domains: Jelly Rolls

Ligands and Environments

2 bound ligands:
Ligand MN 8 x MN
Ligand CA 8 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P1
Unit cell:
a: 78.8Å b: 79.3Å c: 133.3Å
α: 97.1° β: 90.2° γ: 97.5°
R-values:
R R work R free
0.205 0.205 0.265

Quick links

Citations

7 citation in other articles

Force spectroscopy of the double-tethered concanavalin-A mannose bond.
Ratto et al. (2004)
6 more