Research workbench
Structure of protein L7AE bound to a K-turn derived from an archaeal box H/ACA srna
Analyse Structure of protein L7AE bound to a K-turn derived from an archaeal box H/ACA… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1SDS
- Type
- protein + RNA
- Length
- 381 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Box H/ACA srna; 50S ribosomal protein L7AE
- UniProt
- P54066
- Ligands
- CA, K
Structure
x-ray diffraction · 4 distinct chains · 49% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| D, E, F | Box H/ACA srna | rna | 15 | — | — |
| A | 50S ribosomal protein L7AE | protein | 115 | 49% helix, 17% strand | P54066 |
| B | 50S ribosomal protein L7AE | protein | 109 | 49% helix, 17% strand | P54066 |
| C | 50S ribosomal protein L7AE | protein | 112 | 49% helix, 17% strand | P54066 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
6 interfaces between chains.
- E–B · 449 Ų buried · 16 hydrogen bonds · protein-nucleic
- F–C · 435 Ų buried · 15 hydrogen bonds · protein-nucleic
- D–A · 431 Ų buried · 15 hydrogen bonds · protein-nucleic
- F–A · 222 Ų buried · 11 hydrogen bonds · protein-nucleic
- D–C · 220 Ų buried · 10 hydrogen bonds · protein-nucleic
Compared structures
- 1SDS · Structure of protein L7Ae bound to a K-turn derived from an archaeal box H/ACA sRNA · the same entry in another collection · chain C against C, TM-score 1.00
- P54066 · AlphaFold monomer V2.0 prediction for 50S ribosomal protein L7AE (P54066) · a predicted model of the same protein · chain C against A, TM-score 0.99
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 P54066
- Elsewhere: RCSB PDB 1SDS · PDBe 1SDS · UniProt P54066
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