Research workbench
Structure of a histidine kinase-response regulator complex reveals insights into two-component signaling and a novel cis- autophosphorylation mechanism
Analyse Structure of a histidine kinase-response regulator complex reveals insights… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3DGE
- Type
- protein
- Length
- 718 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Sensor protein; Response regulator
- EC
- 2.7.13.3
- UniProt
- Q9WZV7, Q9WYT9
- Ligands
- ADP, SO4
- Pockets
- 5 · best druggability 0.83
Structure
x-ray diffraction · 2 distinct chains · 45% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Sensor protein (EC 2.7.13.3) | protein | 237 | 46% helix, 19% strand | Q9WZV7 |
| C, D | Response regulator | protein | 122 | 42% helix, 18% strand | Q9WYT9 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · 2 copies · chains A, B
- SO4 · Sulfate ion · ion · 2 copies · chains A, C, B, D
- CIT · Citric acid · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1063 | 0.83 | 0.84 | 103 | SO4, ADP |
| 2 | 1118 | 0.83 | 0.84 | 105 | SO4, ADP |
| 3 | 259 | 0.64 | 0.82 | 31 | empty |
| 4 | 255 | 0.62 | 0.81 | 31 | empty |
| 5 | 65 | 0.31 | 0.75 | 15 | empty |
Interfaces
5 interfaces between chains.
- A–B · 1890 Ų buried · 9 hydrogen bonds · protein-protein
- B–D · 997 Ų buried · 6 hydrogen bonds · protein-protein
- A–C · 973 Ų buried · 8 hydrogen bonds · protein-protein
- C–B · 290 Ų buried · 5 hydrogen bonds · protein-protein
- A–D · 236 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 3DGE · Structure of a histidine kinase-response regulator complex reveals insights 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 Q9WZV7
- Every structure of UniProt Q9WYT9
- Elsewhere: RCSB PDB 3DGE · PDBe 3DGE · UniProt Q9WZV7 · UniProt Q9WYT9
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