PDBe 2aai

X-ray diffraction
2.5Å resolution

Crystallographic refinement of ricin to 2.5 Angstroms

Released:
Source organism: Ricinus communis
Primary publication:
Crystallographic refinement of ricin to 2.5 A.
Proteins 10 240-50 (1991)
PMID: 1881880

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Ricin A chain Chain: A
Molecule details ›
Chain: A
Length: 267 amino acids
Theoretical weight: 29.94 KDa
Source organism: Ricinus communis
Expression system: Not provided
UniProt:
  • Canonical: P02879 (Residues: 36-302; Coverage: 49%)
Sequence domains: Ribosome inactivating protein
Structure domains:
Ricin B chain Chain: B
Molecule details ›
Chain: B
Length: 262 amino acids
Theoretical weight: 28.99 KDa
Source organism: Ricinus communis
Expression system: Not provided
UniProt:
  • Canonical: P02879 (Residues: 315-576; Coverage: 48%)
Sequence domains: Ricin-type beta-trefoil lectin domain
Structure domains: Trefoil (Acidic Fibroblast Growth Factor, subunit A)

Ligands and Environments


No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 72.74Å b: 78.49Å c: 114.34Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.212 0.212 not available
Expression system: Not provided