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6XVX

X-ray structure obtained upon reaction of dirhodium tetraacetate with RNase A (high resolution)

This is a non-PDB format compatible entry.
Summary for 6XVX
Entry DOI10.2210/pdb6xvx/pdb
DescriptorRibonuclease pancreatic, ACETATE ION, RHODIUM(III) ION, ... (4 entities in total)
Functional Keywordsdirhodium, model protein, metalation, unknown function
Biological sourceBos taurus (cattle)
Total number of polymer chains2
Total formula weight29243.65
Authors
Merlino, A.,Ferraro, G. (deposition date: 2020-01-22, release date: 2020-02-19, Last modification date: 2024-11-20)
Primary citationFerraro, G.,Pratesi, A.,Messori, L.,Merlino, A.
Protein interactions of dirhodium tetraacetate: a structural study.
Dalton Trans, 49:2412-2416, 2020
Cited by
PubMed Abstract: The interactions between the cytotoxic paddlewheel dirhodium complex [Rh2(μ-O2CCH3)4] and the model protein bovine pancreatic ribonuclease (RNase A) were investigated by high-resolution mass spectrometry and X-ray crystallography. The results indicate that [Rh2(μ-O2CCH3)4] extensively reacts with RNase A. The metal compound binds the protein via coordination of the imidazole ring of a His side chain to one of its axial sites, while the dirhodium center and the acetato ligands remain unmodified. Data provide valuable information for the design of artificial dirhodium-containing metalloenzymes.
PubMed: 32022076
DOI: 10.1039/c9dt04819g
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.4 Å)
Structure validation

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