Research workbench
Structure of the cytoplasmic segment of histidine kinase qsec
Analyse Structure of the cytoplasmic segment of histidine kinase qsec in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3JZ3
- Type
- protein
- Length
- 310 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Sensor protein qsec
- EC
- 2.7.13.3
- UniProt
- P40719
- Ligands
- SO4
- Pockets
- 2 · best druggability 0.69
Structure
x-ray diffraction · 2 distinct chains · 40% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Sensor protein qsec (EC 2.7.13.3) | protein | 151 | 40% helix, 25% strand | P40719 |
| B | Sensor protein qsec (EC 2.7.13.3) | protein | 159 | 40% helix, 25% strand | P40719 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 153 | 0.69 | 0.89 | 26 | empty |
| 2 | 105 | 0.43 | 0.77 | 24 | empty |
Interfaces
1 interface between chains.
- A–B · 1644 Ų buried · 18 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 modified (engineered).
Compared structures
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 P40719
- Elsewhere: RCSB PDB 3JZ3 · PDBe 3JZ3 · UniProt P40719
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