PDBe 2qes

X-ray diffraction
1.24Å resolution

Crystal structure of the ribosome inactivating protein PDL4 from P. dioica leaves in complex with adenine

Released:

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)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ribosome-inactivating protein PD-L3/PD-L4 Chain: A
Molecule details ›
Chain: A
Length: 261 amino acids
Theoretical weight: 29.22 KDa
Source organism: Phytolacca dioica
UniProt:
  • Canonical: P84854 (Residues: 1-261; Coverage: 100%)
Sequence domains: Ribosome inactivating protein
Structure domains:

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE BW7A
Spacegroup: P212121
Unit cell:
a: 43.521Å b: 58.813Å c: 98.774Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.116 0.116 0.145