› 1mrk

X-ray diffraction
1.6Å resolution

STUDIES ON CRYSTAL STRUCTURES ACTIVE CENTER GEOMETRY AND DEPURINE MECHANISM OF TWO RIBOSOME-INACTIVATING PROTEINS

Released:
DOI: 10.2210/pdb1mrk/pdb
PDB entry 1mrk coloured by chain, front view.
PDB entry 1mrk coloured by chain, side view.
PDB entry 1mrk coloured by chain, top view.
Source organism: Trichosanthes kirilowii
Primary publication:
Studies on crystal structures, active-centre geometry and depurinating mechanism of two ribosome-inactivating proteins.
Huang Q, Liu S, Tang Y, Jin S, Wang Y
Biochem J 309 ( Pt 1) 285-98 (1995)
PMID: 7619070

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-531389 (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
Expression system: Not provided
UniProt:
  • Canonical: P09989 (Residues: 24-270; Coverage: 93%)
Sequence domains: Ribosome inactivating protein
Structure domains:

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 38.24Å b: 76.74Å c: 79.25Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.176 0.176 not available
Expression system: Not provided

Quick links

Citations

3 review citations

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

6 mentions without citation

LIGSITEcsc: predicting ligand binding sites using the Connolly surface and degree of conservation.
Huang et al. (2006)
5 more