› 1bry

X-ray diffraction
2.1Å 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
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-152554 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ribosome-inactivating protein bryodin I Chains: Y, Z
Molecule details ›
Chains: Y, Z
Length: 248 amino acids
Theoretical weight: 27.2 KDa
Source organism: Bryonia dioica
Expression system: Escherichia coli
UniProt:
  • Canonical: P33185 (Residues: 24-270; Coverage: 93%)
Sequence domains: Ribosome inactivating protein
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P212121
Unit cell:
a: 65.72Å b: 77.563Å c: 115.601Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.237 0.237 0.298
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Biological activities of ribosome-inactivating proteins and their possible applications as antimicrobial, anticancer, and anti-pest agents and in neuroscience research.
Akkouh et al. (2015)
2 more

2 mentions without citation

Structures and Ribosomal Interaction of Ribosome-Inactivating Proteins.
Shi et al. (2016)
1 more