Research workbench
PAS domain of histidine kinase ThkA (TM1359)
Analyse PAS domain of histidine kinase ThkA (TM1359) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3A0S
- Type
- protein
- Length
- 96 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.47
- Source
- Thermotoga maritima
- Molecule
- Sensor protein
- EC
- 2.7.13.3
- UniProt
- Q9X180
Structure
x-ray diffraction · resolution 1.47 · 1 distinct chain · 28% helix, 42% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Sensor protein (EC 2.7.13.3) | protein | 96 | 28% helix, 42% strand | Q9X180 |
Ligands and binding sites
- PG4 · Tetraethylene glycol · additive · 4 copies · chains A
- PGE · Triethylene glycol · additive · chains A
- PEG · Di(hydroxyethyl)ether · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 3A0S · Pas domain of histidine kinase thka (TM1359) · 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 Q9X180
- Elsewhere: RCSB PDB 3A0S · PDBe 3A0S · UniProt Q9X180
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