Research workbench
Ttgr in complex with tetracycline
Analyse Ttgr in complex with tetracycline in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2UXO
- Type
- protein
- Length
- 411 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hth-type transcriptional regulator ttgr
- UniProt
- Q9AIU0
- Ligands
- TAC
- Pockets
- 3 · best druggability 0.82
Structure
x-ray diffraction · 2 distinct chains · 74% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hth-type transcriptional regulator ttgr | protein | 206 | 75% helix, 1% strand | Q9AIU0 |
| B | Hth-type transcriptional regulator ttgr | protein | 205 | 73% helix, 1% strand | Q9AIU0 |
Ligands and binding sites
- TAC · Tetracycline · ligand · chains 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, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 583 | 0.82 | 0.87 | 47 | TAC |
| 2 | 512 | 0.82 | 0.88 | 45 | empty |
| 3 | 61 | 0.31 | 0.76 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 2204 Ų buried · 27 hydrogen bonds · protein-protein
Compared structures
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 Q9AIU0
- Elsewhere: RCSB PDB 2UXO · PDBe 2UXO · UniProt Q9AIU0
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