Research workbench
Structural and functional characterisation of partner switching regulating the environmental stress response in bacillus subtilis
Analyse Structural and functional characterisation of partner switching regulating the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2J6Y
- Type
- protein
- Length
- 416 residues
- Chains
- 5
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phosphoserine phosphatase rsbu
- EC
- 3.1.3.3
- UniProt
- P40399
- Pockets
- 4 · best druggability 0.56
Structure
x-ray diffraction · 5 distinct chains · 83% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphoserine phosphatase rsbu (EC 3.1.3.3) | protein | 85 | 84% helix, 0% strand | P40399 |
| B | Phosphoserine phosphatase rsbu (EC 3.1.3.3) | protein | 81 | 84% helix, 0% strand | P40399 |
| C | Phosphoserine phosphatase rsbu (EC 3.1.3.3) | protein | 85 | 79% helix, 0% strand | P40399 |
| D | Phosphoserine phosphatase rsbu (EC 3.1.3.3) | protein | 84 | 85% helix, 0% strand | P40399 |
| E | Phosphoserine phosphatase rsbu (EC 3.1.3.3) | protein | 81 | 84% helix, 0% strand | P40399 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 250 | 0.56 | 0.77 | 30 | empty |
| 2 | 286 | 0.52 | 0.74 | 29 | empty |
| 3 | 86 | 0.39 | 0.77 | 19 | empty |
| 4 | 66 | 0.33 | 0.76 | 14 | empty |
Interfaces
6 interfaces between chains.
- A–B · 1816 Ų buried · 11 hydrogen bonds · protein-protein
- C–D · 1771 Ų buried · 11 hydrogen bonds · protein-protein
- A–C · 376 Ų buried · 5 hydrogen bonds · protein-protein
- B–E · 300 Ų buried · 4 hydrogen bonds · protein-protein
- A–D · 143 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 2J6Y · Structural and Functional Characterisation of partner switching regulating the… · the same entry in another collection · chain E against E, TM-score 1.00
- P40399 · AlphaFold monomer V2.0 prediction for phosphoserine phosphatase rsbu (P40399) · 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 P40399
- Elsewhere: RCSB PDB 2J6Y · PDBe 2J6Y · UniProt P40399
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