2y8y Summary

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STRUCTURE B OF CRISPR ENDORIBONUCLEASE CSE3 BOUND TO 19 NT RNA

The structure was published by Sashital, D.G., Jinek, M., and Doudna, J.A., in 2011 in a paper entitled "An RNA-Induced Conformational Change Required for Crispr RNA Cleavage by the Endoribonuclease Cse3." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.44 Å and deposited in 2011.

The experimental data on which the structure is based was also deposited.

This PDB entry contains a complex of 2 biomacromolecules, namely CSE3 and 5'-R(*UP*CP*CP*CP*CP*AP*CP*GP*CP*GP*UP*GP*UP*GP *GP*GP*DGP*AP*U)-3'.

The molecule most likely forms heterodimers.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):


Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A CSE3 Q53WG9 (1-211) (CAS6_THET8)search Thermus thermophilus HB8search 100% 215 93%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
Q53WG9 (1 - 211) CSE3 Thermus thermophilus HB8

Chain Structural classification (CATH) Sequence family (Pfam)
A (Q53WG9) Crispr-associated protein; domain 1search, Crispr-associated protein; domain 2search PF08798: CRISPR associated proteinsearch

Chain ID Biological process (GO) Molecular function (GO)
A (Q53WG9) nucleic acid phosphodiester bond hydrolysissearch defense response to virussearch metabolic processsearch nuclease activitysearch RNA bindingsearch endonuclease activitysearch hydrolase activitysearch

Chain InterPro annotation
A CRISPR-associated protein Cse3search