Research workbench
Molecular basis of box C/D RNA-protein interaction: co-crystal structure of the archaeal srnp intiation complex
Analyse Molecular basis of box C/D RNA-protein interaction: co-crystal structure of the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1RLG
- Type
- protein + RNA
- Length
- 280 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 25-mer; 50S ribosomal protein L7AE
- UniProt
- O29494
- Pockets
- 1 · best druggability 0.26
Structure
x-ray diffraction · 3 distinct chains · 46% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| C, D | 25-mer | rna | 25 | — | — |
| A | 50S ribosomal protein L7AE | protein | 113 | 49% helix, 17% strand | O29494 |
| B | 50S ribosomal protein L7AE | protein | 117 | 44% helix, 16% strand | O29494 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 53 | 0.26 | 0.74 | 13 | empty |
Interfaces
3 interfaces between chains.
- C–A · 661 Ų buried · 27 hydrogen bonds · protein-nucleic
- D–B · 635 Ų buried · 29 hydrogen bonds · protein-nucleic
- C–D · 189 Ų buried · 11 hydrogen bonds · nucleic-nucleic
Modifications
Observed in the structure: 6 modified (nucleotide modification).
Compared structures
- 1RLG · Molecular basis of Box C/D RNA-protein interaction: co-crystal structure of the Archaeal… · the same entry in another collection · chain C against C, TM-score 1.00
- O29494 · AlphaFold monomer V2.0 prediction for 50S ribosomal protein L7AE (O29494) · a predicted model of the same protein · chain B against A, TM-score 0.98
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt O29494
- Elsewhere: RCSB PDB 1RLG · PDBe 1RLG · UniProt O29494
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