› 8tab

X-ray diffraction
2.26Å resolution

Function and Biology Details

Reaction catalysed: 
Endohydrolysis of the N-glycosidic bond at one specific adenosine on the 28S rRNA.
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-527014 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ricin A chain Chain: A
Molecule details ›
Chain: A
Length: 258 amino acids
Theoretical weight: 28.94 KDa
Source organism: Ricinus communis
Expression system: Escherichia coli
UniProt:
  • Canonical: P02879 (Residues: 39-296; Coverage: 48%)
Sequence domains: Ribosome inactivating protein

Ligands and Environments

4 bound ligands:
Ligand CL 3 x CL
Ligand U4T 1 x U4T
Ligand EDO 2 x EDO
Ligand 2PE 1 x 2PE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-E
Spacegroup: P6322
Unit cell:
a: 169.146Å b: 169.146Å c: 55.913Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.187 0.186 0.219
Expression system: Escherichia coli

Quick links

Citations

2 citation in other articles

A fluorescence anisotropy-based competition assay to identify inhibitors against ricin and Shiga toxin ribosome interactions.
Dutta et al. (2024)
1 more

1 mention without citation

Structure-based design and optimization of a new class of small molecule inhibitors targeting the P-stalk binding pocket of ricin.
Rudolph et al. (2024)