Research workbench
Structural and functional characterisation of partner-switching regulating the environmental stress response in B. 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
- 2J70
- Type
- protein
- Length
- 83 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phosphoserine phosphatase rsbu
- EC
- 3.1.3.3
- UniProt
- P40399
- Pockets
- 1 · best druggability 0.34
Structure
x-ray diffraction · 1 distinct chain · 84% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphoserine phosphatase rsbu (EC 3.1.3.3) | protein | 83 | 84% helix, 0% strand | P40399 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 71 | 0.34 | 0.75 | 16 | empty |
Compared structures
- 2J70 · Structural and functional characterisation of partner-switching regulating the… · the same entry in another collection · chain A against A, TM-score 1.00
- P40399 · AlphaFold monomer V2.0 prediction for phosphoserine phosphatase rsbu (P40399) · a predicted model of the same protein · chain A against A, TM-score 0.96
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 2J70 · PDBe 2J70 · UniProt P40399
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