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X-ray diffraction
3.9Å resolution

Crystal Structure of the Anthrax Lethal Factor (LF): Wild-type LF Complexed with the N-terminal Sequence of MAPKK2

Released:

Function and Biology Details

Reactions catalysed:
Preferred amino acids around the cleavage site can be denoted BBBBxHx-|-H, in which B denotes Arg or Lys, H denotes a hydrophobic amino acid, and x is any amino acid. The only known protein substrates are mitogen-activated protein (MAP) kinase kinases.
ATP + L-seryl/L-threonyl/L-tyrosyl-[protein] = ADP + O-phospho-L-seryl/O-phospho-L-threonyl/O-phospho-L-tyrosyl-[protein]
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-147526 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Lethal factor Chain: A
Molecule details ›
Chain: A
Length: 776 amino acids
Theoretical weight: 90.36 KDa
Source organism: Bacillus anthracis
Expression system: Bacillus anthracis
UniProt:
  • Canonical: P15917 (Residues: 34-809; Coverage: 100%)
Gene names: BXA0172, GBAA_pXO1_0172, lef, pXO1-107
Sequence domains:
Structure domains:
Dual specificity mitogen-activated protein kinase kinase 2 Chain: B
Molecule details ›
Chain: B
Length: 16 amino acids
Theoretical weight: 1.79 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P36507 (Residues: 1-16; Coverage: 4%)
Gene names: MAP2K2, MEK2, MKK2, PRKMK2

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL7-1
Spacegroup: I4132
Unit cell:
a: 330.7Å b: 330.7Å c: 330.7Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.296 0.296 0.316
Expression systems:
  • Bacillus anthracis
  • Not provided