› 1obs

X-ray diffraction
2.2Å resolution

STRUCTURE OF RICIN A CHAIN MUTANT

Released:
DOI: 10.2210/pdb1obs/pdb
PDB entry 1obs coloured by chain, front view.
PDB entry 1obs coloured by chain, side view.
PDB entry 1obs coloured by chain, top view.
Source organism: Ricinus communis
Primary publication:
Structure and activity of an active site substitution of ricin A chain.
Day PJ, Ernst SR, Frankel AE, Monzingo AF, Pascal JM, Molina-Svinth MC, Robertus JD
Biochemistry 35 11098-103 (1996)
PMID: 8780513

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:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-136324 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ricin A chain Chain: A
Molecule details ›
Chain: A
Length: 267 amino acids
Theoretical weight: 29.92 KDa
Source organism: Ricinus communis
Expression system: Escherichia coli
UniProt:
  • Canonical: P02879 (Residues: 36-302; Coverage: 49%)
Sequence domains: Ribosome inactivating protein
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P41212
Unit cell:
a: 68.8Å b: 68.8Å c: 141.2Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.214 0.214 not available
Expression system: Escherichia coli

Quick links

Citations

6 review citations

The history of ricin, abrin and related toxins.
Olsnes S. (2004)
5 more

2 mentions without citation

Stathmin and interfacial microtubule inhibitors recognize a naturally curved conformation of tubulin dimers.
Barbier et al. (2010)
1 more