› 1cq9

X-ray diffraction
3.5Å resolution

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
Molecule details ›
Chains: A, B, C, D
Length: 236 amino acids
Theoretical weight: 25.21 KDa
Source organism: Arachis hypogaea
UniProt:
  • Canonical: P02872 (Residues: 24-259; Coverage: 94%)
Sequence domains: Legume lectin domain
Structure domains: Jelly Rolls

Ligands and Environments

2 bound ligands:
Ligand CA 4 x CA
Ligand MN 4 x MN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P1
Unit cell:
a: 53.64Å b: 71.79Å c: 86.42Å
α: 65.35° β: 77.66° γ: 72.31°
R-values:
R R work R free
0.217 0.217 0.278

Quick links

Citations

4 review citations

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

1 mention without citation

Small molecule inhibitors reveal an indispensable scaffolding role of RIPK2 in NOD2 signaling.
Hrdinka et al. (2018)