X-ray diffraction
2.65Å resolution

H/L (SLPH/SLPL) complex from C. difficile (R7404 strain)


Function and Biology Details

Reaction catalysed:
Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
LMWSLP_N domain-containing protein Chains: A, C
Molecule details ›
Chains: A, C
Length: 317 amino acids
Theoretical weight: 33.82 KDa
Source organism: Clostridioides difficile
  • Canonical: Q8KHI4 (Residues: 7-323; Coverage: 90%)
Gene name: slpA
Sequence domains: Low molecular weight S layer protein N terminal
LMWSLP_N domain-containing protein Chains: B, D
Molecule details ›
Chains: B, D
Length: 373 amino acids
Theoretical weight: 39.45 KDa
Source organism: Clostridioides difficile
  • Canonical: Q9AEM2 (Residues: 342-714; Coverage: 54%)
Gene names: SAMEA1531904_01302, slpA
Sequence domains: ell wall binding domain 2 (CWB2)

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: P21
Unit cell:
a: 78.052Å b: 137.94Å c: 84.734Å
α: 90° β: 100.7° γ: 90°
R R work R free
0.228 0.225 0.278