› 1mrg

X-ray diffraction
1.8Å resolution

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

Released:
DOI: 10.2210/pdb1mrg/pdb
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PDB entry 1mrg coloured by chain, front view.
PDB entry 1mrg coloured by chain, side view.
PDB entry 1mrg coloured by chain, top view.
Source organism: Momordica charantia
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-147607 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ribosome-inactivating protein momordin I Chain: A
Molecule details ›
Chain: A
Length: 263 amino acids
Theoretical weight: 29.13 KDa
Source organism: Momordica charantia
Expression system: Not provided
UniProt:
  • Canonical: P16094 (Residues: 24-286; Coverage: 100%)
Sequence domains: Ribosome inactivating protein
Structure domains:

Ligands and Environments

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

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
Spacegroup: R3
Unit cell:
a: 131.6Å b: 131.6Å c: 39.7Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.195 0.195 not available
Expression system: Not provided

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Citations

3 review citations

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

11 mentions without citation

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

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