PDBe 1pwv

X-ray diffraction
2.85Å resolution

Crystal structure of Anthrax Lethal Factor wild-type protein complexed with an optimised peptide substrate.

Released:

Function and Biology Details

Reaction 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. 
Biochemical function:
Cellular component:

Structure analysis Details

Assemblies composition:
hetero dimer (preferred)
hetero tetramer
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
LF20 Chains: C, D
Molecule details ›
Chains: C, D
Length: 20 amino acids
Theoretical weight: 2.35 KDa
Source organism: Synthetic construct
Expression system: Not provided
Lethal factor Chains: A, B
Molecule details ›
Chains: A, B
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:

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL1-5
Spacegroup: P21
Unit cell:
a: 96.7Å b: 137.4Å c: 98.3Å
α: 90° β: 98° γ: 90°
R-values:
R R work R free
0.231 0.231 0.279
Expression systems:
  • Not provided
  • Bacillus anthracis