Research workbench
Structure of the chey-BEF3 complex with substitutions at 59 and 89: N59D and E89Q
Analyse Structure of the chey-BEF3 complex with substitutions at 59 and 89: N59D and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3RVJ
- Type
- protein
- Length
- 260 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chemotaxis protein chey
- UniProt
- P0AE67
- Ligands
- BEF, MN, SO4
- Pockets
- 2 · best druggability 0.50
Structure
x-ray diffraction · 1 distinct chain · 45% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Chemotaxis protein chey | protein | 130 | 45% helix, 16% strand | P0AE67 |
Ligands and binding sites
- BEF · Beryllium trifluoride ion · ligand · 2 copies · chains A, B
- MN · Manganese (II) ion · metal · 2 copies · chains A, B
- SO4 · Sulfate ion · ion · 4 copies · chains A, B
- GOL · Glycerol · additive · 12 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, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 213 | 0.50 | 0.76 | 35 | empty |
| 2 | 51 | 0.45 | 0.84 | 12 | empty |
Interfaces
1 interface between chains.
- A–B · 614 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 3RVJ · Structure of the CheY-BeF3 Complex with substitutions at 59 and 89: N59D and E89Q · the same entry in another collection · chain A against A, TM-score 1.00
- P0AE67 · AlphaFold monomer V2.0 prediction for chemotaxis protein chey (P0AE67) · 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 P0AE67
- Elsewhere: RCSB PDB 3RVJ · PDBe 3RVJ · UniProt P0AE67
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