2z8o

X-ray diffraction
2.4Å resolution

Structural basis for the catalytic mechanism of phosphothreonine lyase

Released:

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
MAPK phosphothreonine lyase Chains: A, B
Molecule details ›
Chains: A, B
Length: 241 amino acids
Theoretical weight: 28.1 KDa
Source organism: Salmonella enterica subsp. enterica serovar Typhimurium
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P0A2M9 (Residues: 1-241; Coverage: 100%)
Gene names: PSLT038, mkaD, spvC, vsdD
Sequence domains: Salmonella virulence-associated 28kDa protein
Structure domains: phosphothreonine lyase

Ligands and Environments

1 bound ligand:

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P4122
Unit cell:
a: 70.755Å b: 70.755Å c: 200.71Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.243 0.243 0.253
Expression system: Escherichia coli BL21