Research workbench
The structure of a histidine kinase-response regulator complex sheds light into two-component signaling and reveals a novel cis autophosphorylation mechanism
Analyse The structure of a histidine kinase-response regulator complex sheds light into… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3GL9
- Type
- protein
- Length
- 481 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Response regulator
- UniProt
- Q9WYT9
- Ligands
- MG, SO4
- Pockets
- 1 · best druggability 0.64
Structure
x-ray diffraction · 2 distinct chains · 43% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, D | Response regulator | protein | 120 | 43% helix, 20% strand | Q9WYT9 |
| B | Response regulator | protein | 121 | 43% helix, 20% strand | Q9WYT9 |
Ligands and binding sites
- MG · Magnesium ion · metal · 4 copies · chains A, B, C, D
- SO4 · Sulfate ion · ion · 5 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 481 | 0.64 | 0.77 | 55 | SO4 |
Interfaces
4 interfaces between chains.
- B–C · 650 Ų buried · 3 hydrogen bonds · protein-protein
- A–C · 628 Ų buried · 4 hydrogen bonds · protein-protein
- C–D · 487 Ų buried · 7 hydrogen bonds · protein-protein
- A–D · 57 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 modified (nonstandard).
Compared structures
- 3GL9 · The structure of a histidine kinase-response regulator complex sheds light into… · 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 Q9WYT9
- Elsewhere: RCSB PDB 3GL9 · PDBe 3GL9 · UniProt Q9WYT9
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