Research workbench
Pas domain of histidine kinase thka (TM1359) (semet, F486M/F489M)
Analyse Pas domain of histidine kinase thka (TM1359) (semet, F486M/F489M) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3A0V
- Type
- protein
- Length
- 96 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Sensor protein
- EC
- 2.7.13.3
- UniProt
- Q9X180
Structure
x-ray diffraction · 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
- EOH · Ethanol · additive · 4 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 3 modified (engineered).
Compared structures
- 3A0V · PAS domain of histidine kinase ThkA (TM1359) (SeMet, F486M/F489M) · 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 3A0V · PDBe 3A0V · UniProt Q9X180
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