Research workbench
Structural basis for targeting and elongation arrest of bacillus signal recognition particle
Analyse Structural basis for targeting and elongation arrest of bacillus signal… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4UE4
- Type
- protein + RNA
- Length
- 390 residues
- Chains
- 3
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P37105
Structure
electron microscopy · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | rna | 266 | — | — |
| B | — | protein | 22 | — | — |
| C | — | protein | 102 | — | P37105 |
Compared structures
- 4UE4 · Structural basis for targeting and elongation arrest of Bacillus signal recognition… · the same entry in another collection · chain A against A, TM-score 1.00
- P37105 · AlphaFold monomer V2.0 prediction for signal recognition particle protein (P37105) · a predicted model of the same protein · chain C against A, TM-score 0.76
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 P37105
- Elsewhere: RCSB PDB 4UE4 · PDBe 4UE4 · UniProt P37105
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