Research workbench
Co-complex of the histidine kinase region of rets and the dimerization and histidine phosphotransfer domain of gacs
Analyse Co-complex of the histidine kinase region of rets and the dimerization and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7N0E
- Type
- protein
- Length
- 255 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histidine kinase
- EC
- 2.7.13.3
- UniProt
- A0A6A9JSD6, A0A2V3GQV5
- Pockets
- 3 · best druggability 0.51
Structure
x-ray diffraction · 2 distinct chains · 62% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | Histidine kinase (EC 2.7.13.3) | protein | 195 | 54% helix, 24% strand | A0A6A9JSD6 |
| A | Histidine kinase (EC 2.7.13.3) | protein | 60 | 88% helix, 0% strand | A0A2V3GQV5 |
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 | 229 | 0.51 | 0.76 | 24 | empty |
| 2 | 58 | 0.48 | 0.84 | 14 | empty |
| 3 | 62 | 0.37 | 0.78 | 13 | empty |
Interfaces
1 interface between chains.
- B–A · 1349 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 modified (engineered).
Compared structures
- 7N0E · Co-complex of the histidine kinase region of RetS and the dimerization and histidine… · the same entry in another collection · chain B against B, 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 A0A6A9JSD6
- Every structure of UniProt A0A2V3GQV5
- Elsewhere: RCSB PDB 7N0E · PDBe 7N0E · UniProt A0A6A9JSD6 · UniProt A0A2V3GQV5
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