Research workbench
BEF3 activated drrd receiver domain
Analyse BEF3 activated drrd receiver domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3NNN
- Type
- protein
- Length
- 238 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA binding response regulator D
- UniProt
- Q9WYN0
- Ligands
- BEF, MG
- Pockets
- 2 · best druggability 0.57
Structure
x-ray diffraction · 1 distinct chain · 46% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | DNA binding response regulator D | protein | 119 | 46% helix, 19% strand | Q9WYN0 |
Ligands and binding sites
- BEF · Beryllium trifluoride ion · ligand · 2 copies · chains A, B
- MG · Magnesium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 50 | 0.57 | 0.91 | 12 | empty |
| 2 | 103 | 0.41 | 0.78 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 1029 Ų buried · 31 hydrogen bonds · protein-protein
Compared structures
- 3NNN · BeF3 Activated DrrD Receiver Domain · 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 Q9WYN0
- Elsewhere: RCSB PDB 3NNN · PDBe 3NNN · UniProt Q9WYN0
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