Research workbench
Crystal structure of R275E mutant of bmrr bound to DNA and rhodamine
Analyse Crystal structure of R275E mutant of bmrr bound to DNA and rhodamine in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3D6Z
- Type
- protein + DNA
- Length
- 301 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P39075
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | — | dna | 24 | — | — |
| A | — | protein | 277 | — | P39075 |
Compared structures
- 3D6Z · Crystal structure of R275E mutant of BMRR bound to DNA and rhodamine · the same entry in another collection · chain B against B, TM-score 1.00
- P39075 · AlphaFold monomer V2.0 prediction for multidrug-efflux transporter 1 regulator (P39075) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 3D6Z · PDBe 3D6Z · UniProt P39075
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