Research workbench
Structure of the phosphatase domain of the cell fate determinant spoiie from bacillus subtilis
Analyse Structure of the phosphatase domain of the cell fate determinant spoiie from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3T91
- Type
- protein
- Length
- 429 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Stage II sporulation protein E
- EC
- 3.1.3.16
- UniProt
- P37475
- Ligands
- GL0, MAN, MN
- Pockets
- 3 · best druggability 0.63
Structure
x-ray diffraction · 2 distinct chains · 26% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Stage II sporulation protein E (EC 3.1.3.16) | protein | 210 | 25% helix, 34% strand | P37475 |
| B | Stage II sporulation protein E (EC 3.1.3.16) | protein | 219 | 27% helix, 34% strand | P37475 |
Ligands and binding sites
- GL0 · beta-D-gulopyranose · ligand · chains A, B
- MAN · alpha-D-mannopyranose · sugar · chains A, B
- MN · Manganese (II) ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 222 | 0.63 | 0.83 | 41 | GL0, MAN |
| 2 | 258 | 0.55 | 0.77 | 46 | empty |
| 3 | 182 | 0.53 | 0.79 | 30 | empty |
Interfaces
1 interface between chains.
- A–B · 4706 Ų buried · 111 hydrogen bonds · protein-protein
Compared structures
- 3T91 · Structure of the Phosphatase Domain of the Cell Fate Determinant SpoIIE from Bacillus… · the same entry in another collection · chain A against A, TM-score 1.00
- P37475 · AlphaFold monomer V2.0 prediction for stage II sporulation protein E (P37475) · a predicted model of the same protein · chain A against A, TM-score 0.67
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 P37475
- Elsewhere: RCSB PDB 3T91 · PDBe 3T91 · UniProt P37475
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