Research workbench
Crystal structure of the receiver domain of desr in complex with beryllofluoride and magnesium
Analyse Crystal structure of the receiver domain of desr in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4LE0
- Type
- protein
- Length
- 265 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transcriptional regulatory protein desr
- UniProt
- O34723
- Ligands
- BEF, MG
- Pockets
- 1 · best druggability 0.41
Structure
x-ray diffraction · 2 distinct chains · 42% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transcriptional regulatory protein desr | protein | 132 | 42% helix, 22% strand | O34723 |
| B | Transcriptional regulatory protein desr | protein | 133 | 42% helix, 22% strand | O34723 |
Ligands and binding sites
- BEF · Beryllium trifluoride ion · ligand · 2 copies · chains A, B
- MG · Magnesium ion · metal · 2 copies · chains A, B
- ACT · Acetate ion · additive · 2 copies · chains A, B
- GOL · Glycerol · additive · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 105 | 0.41 | 0.77 | 18 | MG, BEF |
Interfaces
1 interface between chains.
- A–B · 923 Ų buried · 16 hydrogen bonds · protein-protein
Compared structures
- 4LE0 · Crystal structure of the receiver domain of DesR in complex with beryllofluoride and… · the same entry in another collection · chain A against A, TM-score 1.00
- O34723 · AlphaFold monomer V2.0 prediction for transcriptional regulatory protein desr (O34723) · a predicted model of the same protein · chain B against A, TM-score 0.96
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 O34723
- Elsewhere: RCSB PDB 4LE0 · PDBe 4LE0 · UniProt O34723
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