Research workbench
Directed evolution of a biosensor selective for the macrolide antibiotic clarithromycin
Analyse Directed evolution of a biosensor selective for the macrolide antibiotic… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6U18
- Type
- protein
- Length
- 367 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Erythromycin resistance repressor protein
- UniProt
- Q9EVJ6
- Ligands
- CTY
- Pockets
- 2 · best druggability 0.79
Structure
x-ray diffraction · 2 distinct chains · 73% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Erythromycin resistance repressor protein | protein | 185 | 73% helix, 0% strand | Q9EVJ6 |
| B | Erythromycin resistance repressor protein | protein | 182 | 73% helix, 0% strand | Q9EVJ6 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 762 | 0.79 | 0.83 | 42 | CTY |
| 2 | 832 | 0.79 | 0.82 | 46 | CTY |
Interfaces
1 interface between chains.
- A–B · 1523 Ų buried · 23 hydrogen bonds · protein-protein
Compared structures
- 6U18 · Directed evolution of a biosensor selective for the macrolide antibiotic clarithromycin · 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 Q9EVJ6
- Elsewhere: RCSB PDB 6U18 · PDBe 6U18 · UniProt Q9EVJ6
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