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Equivalence class NR_20.0_57839.4 Obsolete

#IFEStandardized nameMoleculeOrganismSourceRfamTitleMethodÅDate
13J92|1|5+ 3J92|1|8 (rep)Large subunit ribosomal RNA + 5.8S ribosomal RNA28S rRNA, 5.8S rRNAOryctolagus cuniculusEukaryaRF02543 + RF00002Structure and assembly pathway of the ribosome quality control complexElectron microscopy3.62015-01-21
23JAJ|1|5+ 3JAJ|1|8Large subunit ribosomal RNA + 5.8S ribosomal RNA28S ribosomal RNA, 5.8S ribosomal RNAOryctolagus cuniculusEukaryaRF02543 + RF00002Structure of the engaged state of the mammalian SRP-ribosome complexElectron microscopy3.752015-08-05
33JAN|1|5+ 3JAN|1|8Large subunit ribosomal RNA + 5.8S ribosomal RNA28S ribosomal RNA, 5.8S ribosomal RNAOryctolagus cuniculusEukaryaRF02543 + RF00002Structure of the scanning state of the mammalian SRP-ribosome complexElectron microscopy3.752015-08-05
44D5Y|1|2+ 4D5Y|1|3Large subunit ribosomal RNA + 5.8S ribosomal RNA28S Ribosomal RNA, 5.8S Ribosomal RNAOryctolagus cuniculusEukaryaRF02543 + RF00002Cryo-EM structures of ribosomal 80S complexes with termination factors and cricket paralysis virus IRES reveal the IRES in the translocated stateElectron microscopy92015-03-04
54D67|1|2+ 4D67|1|3Large subunit ribosomal RNA + 5.8S ribosomal RNA28S RRNA, 5.8S RRNAOryctolagus cuniculusEukaryaRF02543 + RF00002Cryo-EM structures of ribosomal 80S complexes with termination factors and cricket paralysis virus IRES reveal the IRES in the translocated stateElectron microscopy92015-03-04
64UJC|1|A2+ 4UJC|1|A3Large subunit ribosomal RNA + 5.8S ribosomal RNA28S RIBOSOMAL RNA, 5.8S RIBOSOMAL RNAOryctolagus cuniculusEukaryaRF02543 + RF00002mammalian 80S HCV-IRES initiation complex with eIF5B POST-like stateElectron microscopy9.52014-07-30
74UJE|1|A2+ 4UJE|1|A3Large subunit ribosomal RNA + 5.8S ribosomal RNA28S Ribosomal RNA, 5.8S Ribosomal RNAOryctolagus cuniculusEukaryaRF02543 + RF00002Regulation of the mammalian elongation cycle by 40S subunit rolling: a eukaryotic-specific ribosome rearrangementElectron microscopy6.92014-07-16
84UJD|1|A2+ 4UJD|1|A3Large subunit ribosomal RNA + 5.8S ribosomal RNA28S Ribosomal RNA, 5.8S Ribosomal RNAOryctolagus cuniculusEukaryaRF02543 + RF00002mammalian 80S HCV-IRES initiation complex with eIF5B PRE-like stateElectron microscopy8.92014-07-30

Release history

Release2.35
Date2015-08-07

Parents

This classParent classesRelease idIntersectionAdded to this classOnly in parent
NR_20.0_57839.4NR_all_57839.32.35(6) 4UJE|1|A2+4UJE|1|A3, 4UJD|1|A2+4UJD|1|A3, 4UJC|1|A2+4UJC|1|A3, 4D67|1|2+4D67|1|3, 4D5Y|1|2+4D5Y|1|3, 3J92|1|5+3J92|1|8(2) 3JAN|1|5+3JAN|1|8, 3JAJ|1|5+3JAJ|1|8(0)

Children

This class Descendant classesRelease idIntersectionOnly in this classAdded to child

Heat map of mutual geometric discrepancy, in Angstroms per nucleotide. Instances are ordered to put similar structures near each other. The colorbar ranges from 0 to the maximum observed discrepancy, up to 0.5

#S - ordering by similarity (same as in the heat map).
#SPDBTitleMethodResolutionLength
13JAN|1|5+3JAN|1|8Structure of the scanning state of the mammalian SRP-ribosome complexELECTRON MICROSCOPY3.753658
23JAJ|1|5+3JAJ|1|8Structure of the engaged state of the mammalian SRP-ribosome complexELECTRON MICROSCOPY3.753658
33J92|1|5+3J92|1|8Structure and assembly pathway of the ribosome quality control complexELECTRON MICROSCOPY3.63662
44UJC|1|A2+4UJC|1|A3mammalian 80S HCV-IRES initiation complex with eIF5B POST-like stateELECTRON MICROSCOPY9.53616
54UJE|1|A2+4UJE|1|A3Regulation of the mammalian elongation cycle by 40S subunit rolling: a eukaryotic-specific ribosome rearrangementELECTRON MICROSCOPY6.93616
64UJD|1|A2+4UJD|1|A3mammalian 80S HCV-IRES initiation complex with eIF5B PRE-like stateELECTRON MICROSCOPY8.93616
74D67|1|2+4D67|1|3Cryo-EM structures of ribosomal 80S complexes with termination factors and cricket paralysis virus IRES reveal the IRES in the translocated stateELECTRON MICROSCOPY93616
84D5Y|1|2+4D5Y|1|3Cryo-EM structures of ribosomal 80S complexes with termination factors and cricket paralysis virus IRES reveal the IRES in the translocated stateELECTRON MICROSCOPY93616
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