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
- 4UE5
- Type
- protein + RNA
- Length
- 1,185 residues
- Chains
- 7
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 7S RNA; SRP14; Signal recognition particle subunit SRP68; Signal recognition particle 54…
- UniProt
- Q00004, P61010, P21262, J9PAS6
- Pockets
- 17 · best druggability 0.71
Structure
electron microscopy · 7 distinct chains · 54% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 7S RNA | rna | 299 | — | — |
| B | SRP14 | protein | 75 | 39% helix, 36% strand | — |
| C | Signal recognition particle subunit SRP68 | protein | 179 | 78% helix, 0% strand | Q00004 |
| D | Signal recognition particle 54 kda protein | protein | 433 | 54% helix, 9% strand | P61010 |
| E | SRP9 | protein | 74 | 39% helix, 34% strand | P21262 |
| F | Signal recognition particle 9 kda protein | protein | 107 | 30% helix, 16% strand | J9PAS6 |
| S | Signal sequence | protein | 18 | 78% helix, 0% strand | — |
Pockets
17 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 937 | 0.71 | 0.77 | 135 | empty |
| 2 | 950 | 0.69 | 0.75 | 96 | empty |
| 3 | 667 | 0.68 | 0.77 | 39 | empty |
| 4 | 1099 | 0.68 | 0.74 | 119 | empty |
| 5 | 925 | 0.67 | 0.74 | 98 | empty |
Interfaces
8 interfaces between chains.
- A–C · 890 Ų buried · 55 hydrogen bonds · protein-nucleic
- B–E · 839 Ų buried · 58 hydrogen bonds · protein-protein
- A–E · 275 Ų buried · 8 hydrogen bonds · protein-nucleic
- A–D · 163 Ų buried · 4 hydrogen bonds · protein-nucleic
- A–B · 154 Ų buried · 2 hydrogen bonds · protein-nucleic
Compared structures
- 4UE5 · Structural basis for targeting and elongation arrest of Bacillus signal recognition… · the same entry in another collection · chain S against S, TM-score 1.00
- Q00004 · AlphaFold monomer V2.0 prediction for signal recognition particle subunit SRP68 (Q00004) · a predicted model of the same protein · chain C against A, TM-score 0.99
- P21262 · AlphaFold monomer V2.0 prediction for signal recognition particle 9 kda protein (P21262) · a predicted model of the same protein · chain E against A, TM-score 0.98
- P61010 · AlphaFold monomer V2.0 prediction for signal recognition particle 54 kda protein (P61010) · a predicted model of the same protein · chain D against A, TM-score 0.85
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 Q00004
- Every structure of UniProt P61010
- Every structure of UniProt P21262
- Every structure of UniProt J9PAS6
- Elsewhere: RCSB PDB 4UE5 · PDBe 4UE5 · UniProt Q00004 · UniProt P61010 · UniProt P21262 · UniProt J9PAS6
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