- Structure title
- Nmd3 is a structural mimic of eIF5A, and activates the cpGTPase Lsg1 during 60S ribosome biogenesis: 60S-Nmd3 Complex
- Authors
- Release date
- 2017-02-08
- Experimental technique
- ELECTRON MICROSCOPY
- Resolution
- 4.2 Å
- Chains
-
3 RNA chains from
Saccharomyces cerevisiae
-
42 other chains
- Nucleic acid compounds
25S Ribosomal RNA, 5S Ribosomal RNA, 5.8S Ribosomal RNA
- Other compounds
60S ribosomal protein L2-A, 60S ribosomal protein L3, 60S ribosomal protein L4-A, 60S ribosomal protein L5, 60S ribosomal protein L6-A, 60S ribosomal protein L7-A, 60S ribosomal protein L8-A, 60S ribosomal protein L9-A, 60S ribosomal protein L10, 60S ribosomal protein L11-A, 60S ribosomal protein L13-A, 60S ribosomal protein L14-A, 60S ribosomal protein L42-A, 60S ribosomal protein L43-A, Ribosomal Protein uL1, Maltose binding protein, 60S ribosomal export protein Nmd3 fusion, 60S ribosomal protein L15-A, 60S ribosomal protein L16-A, 60S ribosomal protein L17-A, 60S ribosomal protein L18-A, 60S ribosomal protein L19-A, 60S ribosomal protein L20-A, 60S ribosomal protein L21-A, 60S ribosomal protein L22-A, 60S ribosomal protein L23-A, 60S ribosomal protein L24-A, 60S ribosomal protein L25, 60S ribosomal protein L26-A, 60S ribosomal protein L27-A, 60S ribosomal protein L28, 60S ribosomal protein L29, 60S ribosomal protein L30, 60S ribosomal protein L31-A, 60S ribosomal protein L32, 60S ribosomal protein L33-A, 60S ribosomal protein L34-A, 60S ribosomal protein L35-A, 60S ribosomal protein L36-A, 60S ribosomal protein L37-A, 60S ribosomal protein L38, 60S ribosomal protein L39, Ubiquitin-60S ribosomal protein L40
Pairwise Interactions
Interactions annotated by
FR3D:
View all
RNA 3D Motifs
In the current release of the
RNA 3D Motif Atlas, 5T6R contains:
-
83 hairpin loops from 0 motif groups
-
164 internal loops from 0 motif groups
-
48 junction loops from 0 motif groups
More
3D Redundancy
5T6R has chains which belong to the following equivalence classes in the current representative set:
Similar structures
None found
