Research workbench
Crystal structure of the chex-chey-BEF3-MG+2 complex from borrelia burgdorferi
Analyse Crystal structure of the chex-chey-BEF3-MG+2 complex from borrelia burgdorferi in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3HZH
- Type
- protein
- Length
- 288 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chemotaxis response regulator (chey-3); Chemotaxis operon protein (chex)
- UniProt
- O51615, O51614
- Ligands
- MG
- Pockets
- 3 · best druggability 0.53
Structure
x-ray diffraction · 2 distinct chains · 37% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chemotaxis response regulator (chey-3) | protein | 134 | 43% helix, 21% strand | O51615 |
| B | Chemotaxis operon protein (chex) | protein | 154 | 32% helix, 26% strand | O51614 |
Ligands and binding sites
- MG · Magnesium ion · metal · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 84 | 0.53 | 0.85 | 21 | empty |
| 2 | 83 | 0.44 | 0.80 | 20 | empty |
| 3 | 99 | 0.44 | 0.78 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 852 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 modified (engineered, nonstandard).
Compared structures
- 3HZH · Crystal structure of the CheX-CheY-BeF3-Mg+2 complex from Borrelia burgdorferi · 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 O51615
- Every structure of UniProt O51614
- Elsewhere: RCSB PDB 3HZH · PDBe 3HZH · UniProt O51615 · UniProt O51614
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