› 1v6m

X-ray diffraction
2.7Å resolution

Peanut Lectin with 9mer peptide (IWSSAGNVA)

Released:
DOI: 10.2210/pdb1v6m/pdb
PDB entry 1v6m coloured by chain, front view.
PDB entry 1v6m coloured by chain, side view.
PDB entry 1v6m coloured by chain, top view.
Source organism: Arachis hypogaea
Primary publication:
Structural plasticity of peanut lectin: an X-ray analysis involving variation in pH, ligand binding and crystal structure.
Kundhavai Natchiar S, Arockia Jeyaprakash A, Ramya TN, Thomas CJ, Suguna K, Surolia A, Vijayan M
Acta Crystallogr D Biol Crystallogr 60 211-9 (2004)
PMID: 14747696

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-136281 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Galactose-binding lectin Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 232 amino acids
Theoretical weight: 24.71 KDa
Source organism: Arachis hypogaea
UniProt:
  • Canonical: P02872 (Residues: 24-255; Coverage: 93%)
Sequence domains: Legume lectin domain
Structure domains: Jelly Rolls

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P21
Unit cell:
a: 127.852Å b: 126.139Å c: 84.825Å
α: 90° β: 116.16° γ: 90°
R-values:
R R work R free
0.21 0.21 0.264

Quick links

Citations

1 review citation

Research advances and prospects of legume lectins.
Katoch et al. (2021)
6 other articles

1 mention without citation

How nature can exploit nonspecific catalytic and carbohydrate binding modules to create enzymatic specificity.
Cuskin et al. (2012)