› 4jlv

X-ray diffraction
2.2Å resolution

Function and Biology Details

Reaction catalysed: 
ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-108820 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Polysaccharide chain length determinant N-terminal domain-containing protein; non-specific protein-tyrosine kinase Chain: A
Molecule details ›
Chain: A
Length: 269 amino acids
Theoretical weight: 30.1 KDa
Source organism: Staphylococcus aureus
Expression system: Escherichia coli
UniProt:
  • Canonical: A8YPQ6 (Residues: 194-222; Coverage: 13%)
  • Canonical: A8YPQ8 (Residues: 1-228; Coverage: 100%)
Gene names: A6760_06995, EP54_05860, EQ90_11680, G6W63_09760, G6Y24_14340, GO793_11520, GO814_11700, GO942_10400, GZ156_01580, GZ163_00605, H2639_06530, HMPREF3211_02682, M1K003_0620, NCTC10702_00308, SAMEA70153168_00860, cap5A, capA, capA1, capB1
Sequence domains: AAA domain
Structure domains: P-loop containing nucleotide triphosphate hydrolases

Ligands and Environments

2 bound ligands:
Ligand ADP 1 x ADP
Ligand MG 1 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P212121
Unit cell:
a: 41.03Å b: 64.63Å c: 88.28Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.199 0.197 0.242
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Exploring the diversity of protein modifications: special bacterial phosphorylation systems.
Mijakovic et al. (2016)
1 more

3 mentions without citation

A tyrosine phosphoregulatory system controls exopolysaccharide biosynthesis and biofilm formation in Vibrio cholerae.
Schwechheimer et al. (2020)
2 more