› 4jmp

X-ray diffraction
1.3Å 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-108819 (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: 29.71 KDa
Source organism: Staphylococcus aureus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q7BSA3 (Residues: 194-220; Coverage: 12%)
  • Canonical: A8YPQ5 (Residues: 1-230; Coverage: 100%)
Gene names: A6760_06255, E1948_09415, E1948_09420, E1948_14180, E1948_14185, EP54_05280, EQ90_06090, G6W63_04605, GO814_09620, GO942_11920, GZ163_07515, SAMEA1531744_01776, SAMEA1531744_01777, SAMEA70245418_00124, cap8A, capA, capA2, capB2, epsD
Sequence domains: AAA domain
Structure domains: P-loop containing nucleotide triphosphate hydrolases

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-2
Spacegroup: P21
Unit cell:
a: 36.332Å b: 88.666Å c: 39.405Å
α: 90° β: 115.35° γ: 90°
R-values:
R R work R free
0.173 0.172 0.191
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

4 mentions without citation

Comparative analysis of the Tyr-kinases CapB1 and CapB2 fused to their cognate modulators CapA1 and CapA2 from Staphylococcus aureus.
Gruszczyk et al. (2013)
3 more