Research workbench
The X-ray crystal structure of fino, a repressor of bacterial conjugation
Analyse The X-ray crystal structure of fino, a repressor of bacterial conjugation in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1DVO
- Type
- protein
- Length
- 152 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fertility inhibition protein O
- UniProt
- P29367
- Pockets
- 2 · best druggability 0.45
Structure
x-ray diffraction · 1 distinct chain · 67% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fertility inhibition protein O | protein | 152 | 67% helix, 8% strand | P29367 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 150 | 0.45 | 0.76 | 17 | empty |
| 2 | 127 | 0.40 | 0.75 | 17 | empty |
Compared structures
- 1DVO · The X-ray crystal structure of fino, a repressor of bacterial conjugation · the same entry in another collection · chain A against A, TM-score 1.00
- P29367 · AlphaFold monomer V2.0 prediction for fertility inhibition protein (P29367) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P29367
- Elsewhere: RCSB PDB 1DVO · PDBe 1DVO · UniProt P29367
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