Research workbench
The bacterial stressosome: a modular system that has been adapted to control secondary messenger signaling
Analyse The bacterial stressosome: a modular system that has been adapted to control… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3ZTB
- Type
- protein
- Length
- 228 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Anti-sigma-factor antagonist (stas) domain protein
- UniProt
- Q2RIF5
- Ligands
- IOD
- Pockets
- 4 · best druggability 0.43
Structure
x-ray diffraction · 2 distinct chains · 43% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Anti-sigma-factor antagonist (stas) domain protein | protein | 114 | 41% helix, 18% strand | Q2RIF5 |
| B | Anti-sigma-factor antagonist (stas) domain protein | protein | 114 | 44% helix, 18% strand | Q2RIF5 |
Ligands and binding sites
- IOD · Iodide ion · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 75 | 0.43 | 0.81 | 13 | empty |
| 2 | 54 | 0.43 | 0.82 | 16 | empty |
| 3 | 124 | 0.40 | 0.75 | 25 | empty |
| 4 | 50 | 0.25 | 0.73 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 499 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (phosphorylation).
Compared structures
- 3ZTB · The bacterial stressosome: a modular system that has been adapted to control secondary… · the same entry in another collection · chain A against A, TM-score 1.00
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 Q2RIF5
- Elsewhere: RCSB PDB 3ZTB · PDBe 3ZTB · UniProt Q2RIF5
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