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Crystal structure of bmrr bound to ethidium
Analyse Crystal structure of bmrr bound to ethidium in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3Q2Y
- Type
- protein + DNA
- Length
- 299 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Multidrug-efflux transporter 1 regulator; 23 bp promoter
- UniProt
- P39075
- Ligands
- ET
- Pockets
- 2 · best druggability 0.70
Structure
x-ray diffraction · 2 distinct chains · 39% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Multidrug-efflux transporter 1 regulator | protein | 276 | 39% helix, 24% strand | P39075 |
| B | 23 bp promoter | dna | 23 | — | — |
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 | 312 | 0.70 | 0.84 | 43 | empty |
| 2 | 201 | 0.53 | 0.77 | 24 | ET |
Interfaces
1 interface between chains.
- A–B · 349 Ų buried · 8 hydrogen bonds · protein-nucleic
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 P39075
- Elsewhere: RCSB PDB 3Q2Y · PDBe 3Q2Y · UniProt P39075
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