Research workbench
Crystal structure of putative ecf-type sigma factor negative effector from bacillus cereus
Analyse Crystal structure of putative ecf-type sigma factor negative effector from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3FGG
- Type
- protein
- Length
- 293 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Uncharacterized protein BCE2196
- UniProt
- Q739E5
- Ligands
- ZN
- Pockets
- 6 · best druggability 0.61
Structure
x-ray diffraction · 2 distinct chains · 79% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Uncharacterized protein BCE2196 | protein | 147 | 79% helix, 1% strand | Q739E5 |
| B | Uncharacterized protein BCE2196 | protein | 146 | 79% helix, 1% strand | Q739E5 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 478 | 0.61 | 0.75 | 41 | ZN, GOL |
| 2 | 401 | 0.58 | 0.75 | 37 | GOL |
| 3 | 74 | 0.33 | 0.75 | 19 | empty |
| 4 | 68 | 0.33 | 0.75 | 15 | GOL |
| 5 | 70 | 0.31 | 0.74 | 15 | GOL |
Interfaces
1 interface between chains.
- A–B · 532 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 18 modified (engineered).
Compared structures
- 3FGG · Crystal Structure of Putative ECF-type Sigma Factor Negative Effector from Bacillus cereus · 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 Q739E5
- Elsewhere: RCSB PDB 3FGG · PDBe 3FGG · UniProt Q739E5
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