Function and Biology Details
Reaction catalysed:
ATP + protein L-histidine = ADP + protein N-phospho-L-histidine
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
Chemotaxis phosphorelay complex CheA-CheY (preferred)
PDBe Complex ID:
PDB-CPX-139568 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Chemotaxis protein CheY
Molecule details ›
Chains: A, B
Length: 128 amino acids
Theoretical weight: 13.98 KDa
Source organism: Escherichia coli
UniProt:
Sequence domains: Response regulator receiver domain
Structure domains: Rossmann fold
Length: 128 amino acids
Theoretical weight: 13.98 KDa
Source organism: Escherichia coli
UniProt:
- Canonical:
P0AE67 (Residues: 2-129; Coverage: 99%)
Sequence domains: Response regulator receiver domain
Structure domains: Rossmann fold
Chemotaxis protein CheA
Molecule details ›
Chains: C, D
Length: 74 amino acids
Theoretical weight: 8.02 KDa
Source organism: Escherichia coli
UniProt:
Sequence domains: CheY binding
Structure domains: CheY-binding domain of CheA
Length: 74 amino acids
Theoretical weight: 8.02 KDa
Source organism: Escherichia coli
UniProt:
- Canonical: P07363 (Residues: 156-228; Coverage: 11%)
Sequence domains: CheY binding
Structure domains: CheY-binding domain of CheA
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
SSRL BEAMLINE BL9-1
Spacegroup:
P212121
