Research workbench
Crystal structure of chea-289, a signal transducing histidine kinase
Analyse Crystal structure of chea-289, a signal transducing histidine kinase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1B3Q
- Type
- protein
- Length
- 738 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein (chemotaxis protein chea)
- EC
- 2.7.3.-
- UniProt
- Q56310
- Ligands
- HG
- Pockets
- 6 · best druggability 0.66
Structure
x-ray diffraction · 2 distinct chains · 36% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein (chemotaxis protein chea) (EC 2.7.3.-) | protein | 368 | 36% helix, 34% strand | Q56310 |
| B | Protein (chemotaxis protein chea) (EC 2.7.3.-) | protein | 370 | 36% helix, 33% strand | Q56310 |
Ligands and binding sites
- HG · Mercury (II) ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 249 | 0.66 | 0.83 | 28 | empty |
| 2 | 479 | 0.65 | 0.77 | 58 | empty |
| 3 | 223 | 0.62 | 0.81 | 27 | empty |
| 4 | 187 | 0.61 | 0.83 | 33 | empty |
| 5 | 239 | 0.50 | 0.75 | 40 | empty |
Interfaces
1 interface between chains.
- A–B · 2033 Ų buried · 23 hydrogen bonds · protein-protein
Compared structures
- 1B3Q · Crystal structure of chea-289, a signal transducing histidine kinase · the same entry in another collection · chain B against B, TM-score 1.00
- Q56310 · AlphaFold monomer V2.0 prediction for chemotaxis protein chea (Q56310) · a predicted model of the same protein · chain A against A, TM-score 0.79
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 Q56310
- Elsewhere: RCSB PDB 1B3Q · PDBe 1B3Q · UniProt Q56310
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