› 1qd2

X-ray diffraction
1.86Å resolution

CRYSTAL STRUCTURE OF THE COMPLEX OF TRICHOSANTHIN WITH ADENINE, OBTAINED FROM TRICHOSANTHIN COMPLEXED WITH THE DINUCLEOTIDE APG

Released:
DOI: 10.2210/pdb1qd2/pdb
PDB entry 1qd2 coloured by chain, front view.
PDB entry 1qd2 coloured by chain, side view.
PDB entry 1qd2 coloured by chain, top view.
Source organism: Trichosanthes kirilowii
Primary publication:
Crystal structures of the complexes of trichosanthin with four substrate analogs and catalytic mechanism of RNA N-glycosidase.
Gu YJ, Xia ZX
Proteins 39 37-46 (2000)
PMID: 10737925

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-140879 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ribosome-inactivating protein alpha-trichosanthin Chain: A
Molecule details ›
Chain: A
Length: 247 amino acids
Theoretical weight: 27.17 KDa
Source organism: Trichosanthes kirilowii
UniProt:
  • Canonical: P09989 (Residues: 24-270; Coverage: 93%)
Sequence domains: Ribosome inactivating protein
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand ADE 1 x ADE
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 38.41Å b: 76.72Å c: 79.45Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.163 0.163 0.221

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Citations

4 review citations

Recent advances in trichosanthin, a ribosome-inactivating protein with multiple pharmacological properties.
Shaw et al. (2005)
3 more

3 mentions without citation

Plant Ribosome-Inactivating Proteins: Progesses, Challenges and Biotechnological Applications (and a Few Digressions).
Fabbrini et al. (2017)
2 more