› 3lei

X-ray diffraction
1.9Å resolution

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-173871 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thiol-activated cytolysin Chain: A
Molecule details ›
Chain: A
Length: 153 amino acids
Theoretical weight: 16.87 KDa
Source organism: Streptococcus mitis
Expression system: Escherichia coli
UniProt:
  • Canonical: Q2PHL4 (Residues: 38-190; Coverage: 24%)
Gene names: SMNM65_03180, samhpaf, sm-hpaf
Sequence domains: F5/8 type C domain
Structure domains: Galactose-binding domain-like

Ligands and Environments

3 bound ligands:
Ligand FUC 1 x FUC
Ligand CA 1 x CA
Ligand NI 1 x NI
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P43212
Unit cell:
a: 67.01Å b: 67.01Å c: 97.8Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.202 0.199 0.247
Expression system: Escherichia coli

Quick links

Citations

10 review citations

Pore-forming toxins: ancient, but never really out of fashion.
Dal Peraro et al. (2016)
9 more

3 mentions without citation

Structural Basis of the Pore-Forming Toxin/Membrane Interaction.
Li et al. (2021)
2 more