2q8y

X-ray diffraction
2Å resolution

Structural insight into the enzymatic mechanism of the phophothreonine lyase

Released:

Function and Biology Details

Reaction catalysed:
ATP + a protein = ADP + a phosphoprotein
Biochemical function:
Biological process:
  • not assigned
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-141070 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
MAPK phosphothreonine lyase Chain: A
Molecule details ›
Chain: A
Length: 241 amino acids
Theoretical weight: 27.62 KDa
Source organism: Salmonella enterica subsp. enterica serovar Enteritidis
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P0A2N1 (Residues: 1-241; Coverage: 100%)
Gene names: mkaD, spvC, vsdD
Sequence domains: Salmonella virulence-associated 28kDa protein
Structure domains: phosphothreonine lyase
Mitogen-activated protein kinase 7 Chain: B
Molecule details ›
Chain: B
Length: 9 amino acids
Theoretical weight: 1.31 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: Q13164 (Residues: 215-223; Coverage: 1%)
Gene names: BMK1, ERK5, MAPK7, PRKM7

Ligands and Environments

No bound ligands
2 modified residues:

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007
Spacegroup: P212121
Unit cell:
a: 37.367Å b: 71.842Å c: 96.06Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.185 0.181 0.217
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided