1h8g

X-ray diffraction
2.4Å resolution

C-terminal domain of the major autolysin (C-LytA) from Streptococcus pneumoniae

Released:

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 domain:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139118 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Autolysin Chains: A, B
Molecule details ›
Chains: A, B
Length: 95 amino acids
Theoretical weight: 11.15 KDa
Source organism: Streptococcus pneumoniae
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P06653 (Residues: 224-318; Coverage: 30%)
Gene names: SP_1937, lytA
Sequence domains:
Structure domains: Cholin Binding

Ligands and Environments

1 bound ligand:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X11
Spacegroup: P41212
Unit cell:
a: 97.571Å b: 97.571Å c: 68.482Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.219 0.219 0.263
Expression system: Escherichia coli BL21