![EMBL European Bioinformatics Institute](/web_guidelines/images/logos/ÀÖÌìÌÃÓÎÏ·ÍøÕ¾/EMBL_EBI_Logo_white.png"){kind=logo}
Function and Biology Details
Reaction catalysed:
ATP + protein L-histidine = ADP + protein N-phospho-L-histidine
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Signal transduction histidine kinase-related protein, C-terminal
- Signal transduction histidine kinase, dimerisation/phosphoacceptor domain
- Histidine kinase/HSP90-like ATPase domain
- Histidine kinase/HSP90-like ATPase superfamily
- Histidine kinase domain
- Signal transduction histidine kinase, dimerisation/phosphoacceptor domain superfamily
- Metallo-dependent phosphatase-like
Structure analysis Details
Assembly composition:
homo dimer (preferred)
Assembly name:
histidine kinase (preferred)
PDBe Complex ID:
PDB-CPX-102430 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
histidine kinase
Molecule details ›
Chains: A, B
Length: 277 amino acids
Theoretical weight: 31.65 KDa
Source organism: Lactiplantibacillus plantarum JDM1
Expression system: Escherichia coli
UniProt:
Sequence domains: Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase
Structure domains:
Length: 277 amino acids
Theoretical weight: 31.65 KDa
Source organism: Lactiplantibacillus plantarum JDM1
Expression system: Escherichia coli
UniProt:
- Canonical:
A0A0M3KKX3 (Residues: 1-193; Coverage: 100%)
Sequence domains: Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase
Structure domains:
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
![Entry percentile scores](/pdbe/entry-files/4u7n_multipercentile_validation.svg")
X-ray source:
SSRF BEAMLINE BL17U
Spacegroup:
P31
Expression system: Escherichia coli
