Research workbench
Tetracycline chelated MG2+-ion initiates helix unwinding for tet repressor induction
Analyse Tetracycline chelated MG2+-ion initiates helix unwinding for tet repressor… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1BJZ
- Type
- protein
- Length
- 194 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tetracycline repressor
- UniProt
- P0ACT4
- Pockets
- 3 · best druggability 0.61
Structure
x-ray diffraction · 1 distinct chain · 73% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tetracycline repressor | protein | 194 | 73% helix, 0% strand | P0ACT4 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 250 | 0.61 | 0.80 | 31 | empty |
| 2 | 56 | 0.31 | 0.75 | 11 | empty |
| 3 | 57 | 0.28 | 0.74 | 13 | empty |
Compared structures
- 1BJZ · Tetracycline chelated MG2+-ion initiates helix unwinding for tet repressor induction · the same entry in another collection · chain A against A, TM-score 1.00
- P0ACT4 · AlphaFold monomer V2.0 prediction for tetracycline repressor protein class D (P0ACT4) · a predicted model of the same protein · chain A against A, TM-score 0.94
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 P0ACT4
- Elsewhere: RCSB PDB 1BJZ · PDBe 1BJZ · UniProt P0ACT4
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