HL_9O3K_205
3D structure
- PDB id
 - 9O3K (explore in PDB, NAKB, or RNA 3D Hub)
 - Description
 - Crystal structure of the wild-type Thermus thermophilus 70S ribosome in complex with macrolide erythromycin, mRNA, aminoacylated A-site Lys-tRNAlys, P-site fMAC-peptidyl-tRNAmet, and deacylated E-site tRNAlys at 2.70A resolution
 - Experimental method
 - X-RAY DIFFRACTION
 - Resolution
 - 2.7 Å
 
Loop
- Sequence
 - ACU(U8U)UU(T6A)A(PSU)
 - Length
 - 9 nucleotides
 - Bulged bases
 - None detected
 - QA status
 - Modified nucleotides: U8U, T6A, PSU
 
Sequence variability
- 
                            If this chain is mapped to an Rfam alignment, the link below will give its sequence variability.
                            
 - R3DSVS
 
Structural variability across Equivalence Class
- 
                            The link below will give the loop's structural variability across the equivalence class for this chain.
                            
 - R3DMCS EC
 
Structural variability across Rfam
- 
                            If this chain is mapped to an Rfam alignment, the link below will give the loop's structural variability between chains mapped to the same Rfam family.
                            
 - R3DMCS Rfam
 
- HL_9O3K_205 not in the Motif Atlas
 - Geometric match to HL_7U2I_104
 - Geometric discrepancy: 0.1413
 - The information below is about HL_7U2I_104
 - Detailed Annotation
 - tRNA anticodon loop
 - Broad Annotation
 - Anticodon loop
 - Motif group
 - HL_06059.7
 - Basepair signature
 - cWW-F-F-F-F-F-F-F
 - Number of instances in this motif group
 - 51
 
Unit IDs
9O3K|1|2w|A|31
  9O3K|1|2w|C|32
  9O3K|1|2w|U|33
  9O3K|1|2w|U8U|34
  9O3K|1|2w|U|35
  9O3K|1|2w|U|36
  9O3K|1|2w|T6A|37
  9O3K|1|2w|A|38
  9O3K|1|2w|PSU|39
Current chains
- Chain 2w
 - A-site Aminoacyl-tRNA Lys-tRNAlys
 
Nearby chains
- Chain 2A
 - Large subunit ribosomal RNA; LSU rRNA
 - Chain 2a
 - Small subunit ribosomal RNA; SSU rRNA
 - Chain 2l
 - 30S ribosomal protein S12
 - Chain 2m
 - 30S ribosomal protein S13
 - Chain 2v
 - MET-LYS-mRNA
 
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